Journal articles: 'Cell organelle'

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Ouellet, Jimmy, and Yves Barral. "Organelle segregation during mitosis: Lessons from asymmetrically dividing cells." Journal of Cell Biology 196, no. 3 (February 6, 2012): 305–13. http://dx.doi.org/10.1083/jcb.201102078.

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Studies on cell division traditionally focus on the mechanisms of chromosome segregation and cytokinesis, yet we know comparatively little about how organelles segregate. Analysis of organelle partitioning in asymmetrically dividing cells has provided insights into the mechanisms through which cells control organelle distribution. Interestingly, these studies have revealed that segregation mechanisms frequently link organelle distribution to organelle growth and formation. Furthermore, in many cases, cells use organelles, such as the endoplasmic reticulum and P granules, as vectors for the segregation of information. Together, these emerging data suggest that the coordination between organelle growth, division, and segregation plays an important role in the control of cell fate inheritance, cellular aging, and rejuvenation, i.e., the resetting of age in immortal lineages.

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TANAKA, Arowu, Fumi KANO, and Masayuki MURATA. "Organelle Inheritance-Cell Cycle Dependent Dynamics of Organelles in Mammalian Cells." Seibutsu Butsuri 42, no. 3 (2002): 116–21. http://dx.doi.org/10.2142/biophys.42.116.

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Evans, David E., and Chris Hawes. "Organelle Biogenesis and Positioning in Plants." Biochemical Society Transactions 38, no. 3 (May 24, 2010): 729–32. http://dx.doi.org/10.1042/bst0380729.

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The biogenesis and positioning of organelles involves complex interacting processes and precise control. Progress in our understanding is being made rapidly as advances in analysing the nuclear and organellar genome and proteome combine with developments in live-cell microscopy and manipulation at the subcellular level. This paper introduces the collected papers resulting from Organelle Biogenesis and Positioning in Plants, the 2009 Biochemical Society Annual Symposium. Including papers on the nuclear envelope and all major organelles, it considers current knowledge and progress towards unifying themes that will elucidate the mechanisms by which cells generate the correct complement of organelles and adapt and change it in response to environmental and developmental signals.

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Mallo, Natalia, Justin Fellows, Carla Johnson, and Lilach Sheiner. "Protein Import into the Endosymbiotic Organelles of Apicomplexan Parasites." Genes 9, no. 8 (August 14, 2018): 412. http://dx.doi.org/10.3390/genes9080412.

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: The organelles of endosymbiotic origin, plastids, and mitochondria, evolved through the serial acquisition of endosymbionts by a host cell. These events were accompanied by gene transfer from the symbionts to the host, resulting in most of the organellar proteins being encoded in the cell nuclear genome and trafficked into the organelle via a series of translocation complexes. Much of what is known about organelle protein translocation mechanisms is based on studies performed in common model organisms; e.g., yeast and humans or Arabidopsis. However, studies performed in divergent organisms are gradually accumulating. These studies provide insights into universally conserved traits, while discovering traits that are specific to organisms or clades. Apicomplexan parasites feature two organelles of endosymbiotic origin: a secondary plastid named the apicoplast and a mitochondrion. In the context of the diseases caused by apicomplexan parasites, the essential roles and divergent features of both organelles make them prime targets for drug discovery. This potential and the amenability of the apicomplexan Toxoplasma gondii to genetic manipulation motivated research about the mechanisms controlling both organelles’ biogenesis. Here we provide an overview of what is known about apicomplexan organelle protein import. We focus on work done mainly in T. gondii and provide a comparison to model organisms.

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Pelham, R. J., J. J. Lin, and Y. L. Wang. "A high molecular mass non-muscle tropomyosin isoform stimulates retrograde organelle transport." Journal of Cell Science 109, no. 5 (May 1, 1996): 981–89. http://dx.doi.org/10.1242/jcs.109.5.981.

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Although non-muscle tropomyosins (TM) have been implicated in various cellular functions, such as stabilization of actin filaments and possibly regulation of organelle transport, their physiological role is still poorly understood. We have probed the role of a high molecular mass isoform of human fibroblast TM, hTM3, in regulating organelle transport by microinjecting an excess amount of bacterially-expressed protein into normal rat kidney (NRK) epithelial cells. The microinjection induced the dramatic retrograde translocation of organelles into the perinuclear area. Microinjection of hTM5, a low molecular mass isoform had no effect on organelle distribution. Fluorescent staining indicated that hTM3 injection stimulated the retrograde movement of both mitochondria and lysosomes. Moreover, both myosin I and cytoplasmic dynein were found to redistribute with the translocated organelles to the perinuclear area, indicating that these organelles were able to move along both microtubules and actin filaments. The involvement of microtubules was further suggested by the partial inhibition of hTM3-induced organelle movement by the microtubule-depolymerizing drug nocodazole. Our results, along with previous genetic and antibody microinjection studies, suggest that hTM3 may be involved in the regulation of organelle transport.

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Esch, Nicholas, Seokwon Jo, Mackenzie Moore, and Emilyn U. Alejandro. "Nutrient Sensor mTOR and OGT: Orchestrators of Organelle Homeostasis in Pancreatic β-Cells." Journal of Diabetes Research 2020 (December 15, 2020): 1–24. http://dx.doi.org/10.1155/2020/8872639.

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The purpose of this review is to integrate the role of nutrient-sensing pathways into β-cell organelle dysfunction prompted by nutrient excess during type 2 diabetes (T2D). T2D encompasses chronic hyperglycemia, hyperlipidemia, and inflammation, which each contribute to β-cell failure. These factors can disrupt the function of critical β-cell organelles, namely, the ER, mitochondria, lysosomes, and autophagosomes. Dysfunctional organelles cause defects in insulin synthesis and secretion and activate apoptotic pathways if homeostasis is not restored. In this review, we will focus on mTORC1 and OGT, two major anabolic nutrient sensors with important roles in β-cell physiology. Though acute stimulation of these sensors frequently improves β-cell function and promotes adaptation to cell stress, chronic and sustained activity disturbs organelle homeostasis. mTORC1 and OGT regulate organelle function by influencing the expression and activities of key proteins, enzymes, and transcription factors, as well as by modulating autophagy to influence clearance of defective organelles. In addition, mTORC1 and OGT activity influence islet inflammation during T2D, which can further disrupt organelle and β-cell function. Therapies for T2D that fine-tune the activity of these nutrient sensors have yet to be developed, but the important role of mTORC1 and OGT in organelle homeostasis makes them promising targets to improve β-cell function and survival.

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Hertle, Alexander P., Benedikt Haberl, and Ralph Bock. "Horizontal genome transfer by cell-to-cell travel of whole organelles." Science Advances 7, no. 1 (January 2021): eabd8215. http://dx.doi.org/10.1126/sciadv.abd8215.

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Recent work has revealed that both plants and animals transfer genomes between cells. In plants, horizontal transfer of entire plastid, mitochondrial, or nuclear genomes between species generates new combinations of nuclear and organellar genomes, or produces novel species that are allopolyploid. The mechanisms of genome transfer between cells are unknown. Here, we used grafting to identify the mechanisms involved in plastid genome transfer from plant to plant. We show that during proliferation of wound-induced callus, plastids dedifferentiate into small, highly motile, amoeboid organelles. Simultaneously, new intercellular connections emerge by localized cell wall disintegration, forming connective pores through which amoeboid plastids move into neighboring cells. Our work uncovers a pathway of organelle movement from cell to cell and provides a mechanistic framework for horizontal genome transfer.

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Okamoto, Koji. "Organellophagy: Eliminating cellular building blocks via selective autophagy." Journal of Cell Biology 205, no. 4 (May 26, 2014): 435–45. http://dx.doi.org/10.1083/jcb.201402054.

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Maintenance of organellar quality and quantity is critical for cellular homeostasis and adaptation to variable environments. Emerging evidence demonstrates that this kind of control is achieved by selective elimination of organelles via autophagy, termed organellophagy. Organellophagy consists of three key steps: induction, cargo tagging, and sequestration, which involve signaling pathways, organellar landmark molecules, and core autophagy-related proteins, respectively. In addition, posttranslational modifications such as phosphorylation and ubiquitination play important roles in recruiting and tailoring the autophagy machinery to each organelle. The basic principles underlying organellophagy are conserved from yeast to mammals, highlighting its biological relevance in eukaryotic cells.

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Walsh, J. B. "Intracellular selection, conversion bias, and the expected substitution rate of organelle genes." Genetics 130, no. 4 (April 1, 1992): 939–46. http://dx.doi.org/10.1093/genetics/130.4.939.

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Abstract A key step in the substitution of a new organelle mutant throughout a population is the generation of germ-line cells homoplasmic for that mutant. Given that each cell typically contains multiple copies of organelles, each of which in turn contains multiple copies of the organelle genome, processes akin to drift and selection in a population are responsible for producing homoplasmic cells. This paper examines the expected substitution rate of new mutants by obtaining the probability that a new mutant is fixed throughout a cell, allowing for arbitrary rates of genome turnover within an organelle and organelle turnover within the cell, as well as (possibly biased) gene conversion and genetic differences in genome and/or organelle replication rates. Analysis is based on a variation of Moran's model for drift in a haploid population. One interesting result is that if the rate of unbiased conversion is sufficiently strong, it creates enough intracellular drift to overcome even strong differences in the replication rates of wild-type and mutant genomes. Thus, organelles with very high conversion rates are more resistant to intracellular selection based on differences in genome replication and/or degradation rates. It is found that the amount of genetic exchange between organelles within the cell greatly influences the probability of fixation. In the absence of exchange, biased gene conversion and/or differences in genome replication rates do not influence the probability of fixation beyond the initial fixation within a single organelle. With exchange, both these processes influence the probability of fixation throughout the entire cell. Generally speaking, exchange between organelles accentuates the effects of directional intracellular forces.(ABSTRACT TRUNCATED AT 250 WORDS)

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Steinberg, G., and M. Schliwa. "Organelle movements in the wild type and wall-less fz;sg;os-1 mutants of Neurospora crassa are mediated by cytoplasmic microtubules." Journal of Cell Science 106, no. 2 (October 1, 1993): 555–64. http://dx.doi.org/10.1242/jcs.106.2.555.

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The cellular basis of organelle transport in filamentous fungi is still unresolved. Here we have studied the intracellular movement of mitochondria and other organelles in the fungus Neurospora crassa. Four different model systems were employed: hyphae, protoplasts, a cell wallless mutant, and experimentally generated small, flattened cell fragments of the mutant cells. Organelle movements were visualized by DIC optics and computer-enhanced video microscopy. In all cell models the transport of organelles was vectorial and saltatory in nature. The mean velocities for mitochondria, particles and nuclei were 1.4, 2.0, and 0.9 microns/s, respectively. Treatment with 10 microM nocodazole for 30 minutes caused a complete disappearance of microtubules and reversibly blocked directed transport of virtually all organelles, whereas cytochalasin D up to 20 microM was without effect. Correlative video and immunofluorescence microscopy of small fragments of wall-less mutant cells revealed a clear match between microtubule distribution and the tracks of moving organelles. We conclude that organelle movement in the filamentous fungus Neurospora crassa is a microtubule-dependent process.

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Chen, Xian-Ming, Steven P. O'Hara, Bing Q. Huang, Jeremy B. Nelson, Jim Jung-Ching Lin, Guan Zhu, Honorine D. Ward, and Nicholas F. LaRusso. "Apical Organelle Discharge by Cryptosporidium parvum Is Temperature, Cytoskeleton, and Intracellular Calcium Dependent and Required for Host Cell Invasion." Infection and Immunity 72, no. 12 (December 2004): 6806–16. http://dx.doi.org/10.1128/iai.72.12.6806-6816.2004.

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ABSTRACT The apical organelles in apicomplexan parasites are characteristic secretory vesicles containing complex mixtures of molecules. While apical organelle discharge has been demonstrated to be involved in the cellular invasion of some apicomplexan parasites, including Toxoplasma gondii and Plasmodium spp., the mechanisms of apical organelle discharge by Cryptosporidium parvum sporozoites and its role in host cell invasion are unclear. Here we show that the discharge of C. parvum apical organelles occurs in a temperature-dependent fashion. The inhibition of parasite actin and tubulin polymerization by cytochalasin D and colchicines, respectively, inhibited parasite apical organelle discharge. Chelation of the parasite's intracellular calcium also inhibited apical organelle discharge, and this process was partially reversed by raising the intracellular calcium concentration by use of the ionophore A23187. The inhibition of parasite cytoskeleton polymerization by cytochalasin D and colchicine and the depletion of intracellular calcium also decreased the gliding motility of C. parvum sporozoites. Importantly, the inhibition of apical organelle discharge by C. parvum sporozoites blocked parasite invasion of, but not attachment to, host cells (i.e., cultured human cholangiocytes). Moreover, the translocation of a parasite protein, CP2, to the host cell membrane at the region of the host cell-parasite interface was detected; an antibody to CP2 decreased the C. parvum invasion of cholangiocytes. These data demonstrate that the discharge of C. parvum sporozoite apical organelle contents occurs and that it is temperature, intracellular calcium, and cytoskeleton dependent and required for host cell invasion, confirming that apical organelles play a central role in C. parvum entry into host cells.

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Nishida, Keiji, Fumi Yagisawa, Haruko Kuroiwa, Toshiyuki Nagata, and Tsuneyoshi Kuroiwa. "Cell Cycle-regulated, Microtubule-independent Organelle Division in Cyanidioschyzon merolae." Molecular Biology of the Cell 16, no. 5 (May 2005): 2493–502. http://dx.doi.org/10.1091/mbc.e05-01-0068.

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Mitochondrial and chloroplast division controls the number and morphology of organelles, but how cells regulate organelle division remains to be clarified. Here, we show that each step of mitochondrial and chloroplast division is closely associated with the cell cycle in Cyanidioschyzon merolae. Electron microscopy revealed direct associations between the spindle pole bodies and mitochondria, suggesting that mitochondrial distribution is physically coupled with mitosis. Interconnected organelles were fractionated under microtubule-stabilizing condition. Immunoblotting analysis revealed that the protein levels required for organelle division increased before microtubule changes upon cell division, indicating that regulation of protein expression for organelle division is distinct from that of cytokinesis. At the mitochondrial division site, dynamin stuck to one of the divided mitochondria and was spatially associated with the tip of a microtubule stretching from the other one. Inhibition of microtubule organization, proteasome activity or DNA synthesis, respectively, induced arrested cells with divided but shrunk mitochondria, with divided and segregated mitochondria, or with incomplete mitochondrial division restrained at the final severance, and repetitive chloroplast division. The results indicated that mitochondrial morphology and segregation but not division depend on microtubules and implied that the division processes of the two organelles are regulated at distinct checkpoints.

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Bridgman, P. C., B. Kachar, and T. S. Reese. "The structure of cytoplasm in directly frozen cultured cells. II. Cytoplasmic domains associated with organelle movements." Journal of Cell Biology 102, no. 4 (April 1, 1986): 1510–21. http://dx.doi.org/10.1083/jcb.102.4.1510.

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The relationship between organelle movement and cytoplasmic structure in cultured fibroblasts or epithelial cells was studied using video-enhanced differential interference contrast microscopy and electron microscopy of directly frozen whole mounts. Two functional cytoplasmic domains are characterized by these techniques. A central domain rich in microtubules is associated with directed as well as Brownian movements of organelles, while a surrounding domain rich in f-actin supports directed but often intermittent organelle movements more distally along small but distinct individual microtubule tracks. Differences in the organization of the cytoplasm near microtubules may explain why organelle movements are typically continuous in central regions but usually intermittent along the small tracks through the periphery. The central type of cytoplasm has a looser cytoskeletal meshwork than the peripheral cytoplasm which might, therefore, interfere less frequently with organelles moving along microtubules there.

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Marshall, Wallace F. "Scaling of Subcellular Structures." Annual Review of Cell and Developmental Biology 36, no. 1 (October 6, 2020): 219–36. http://dx.doi.org/10.1146/annurev-cellbio-020520-113246.

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As cells grow, the size and number of their internal organelles increase in order to keep up with increased metabolic requirements. Abnormal size of organelles is a hallmark of cancer and an important aspect of diagnosis in cytopathology. Most organelles vary in either size or number, or both, as a function of cell size, but the mechanisms that create this variation remain unclear. In some cases, organelle size appears to scale with cell size through processes of relative growth, but in others the size may be set by either active measurement systems or genetic programs that instruct organelle biosynthetic activities to create organelles of a size appropriate to a given cell type.

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van der Bliek, Alexander, and Xinnan Wang. "Organelles and spatial organization of the cell: organelle homeostasis and turnover." Molecular Biology of the Cell 27, no. 6 (March 15, 2016): 873–74. http://dx.doi.org/10.1091/mbc.e15-11-0761.

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Schuldiner, Maya, and Wei Guo. "Editorial overview: Cell organelles: Organelle communication: new means and new views." Current Opinion in Cell Biology 35 (August 2015): v—vi. http://dx.doi.org/10.1016/j.ceb.2015.07.008.

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Schroer, T. A., B. J. Schnapp, T. S. Reese, and M. P. Sheetz. "The role of kinesin and other soluble factors in organelle movement along microtubules." Journal of Cell Biology 107, no. 5 (November 1, 1988): 1785–92. http://dx.doi.org/10.1083/jcb.107.5.1785.

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Kinesin is a force-generating ATPase that drives the sliding movement of microtubules on glass coverslips and the movement of plastic beads along microtubules. Although kinesin is suspected to participate in microtubule-based organelle transport, the exact role it plays in this process is unclear. To address this question, we have developed a quantitative assay that allows us to determine the ability of soluble factors to promote organelle movement. Salt-washed organelles from squid axoplasm exhibited a nearly undetectable level of movement on purified microtubules. Their frequency of movement could be increased greater than 20-fold by the addition of a high speed axoplasmic supernatant. Immunoadsorption of kinesin from this supernatant decreased the frequency of organelle movement by more than 70%; organelle movements in both directions were markedly reduced. Surprisingly, antibody purified kinesin did not promote organelle movement either by itself or when it was added back to the kinesin-depleted supernatant. This result suggested that other soluble factors necessary for organelle movement were removed along with kinesin during immunoadsorption of the supernatant. A high level of organelle motor activity was recovered in a high salt eluate of the immunoadsorbent that contained only little kinesin. On the basis of these results we propose that organelle movement on microtubules involves other soluble axoplasmic factors in addition to kinesin.

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Ockleford, C. D., C. H. Nevard, I. Indans, and C. J. Jones. "Structure and function of the nematosome." Journal of Cell Science 87, no. 1 (February 1, 1987): 27–44. http://dx.doi.org/10.1242/jcs.87.1.27.

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The ultrastructural morphology of human placental and mouse placental nematosomes has been investigated. The description includes a three-dimensional analysis of the shape of the organelles based on serial sectioning, measurements of the repeat distance of the subunit fibre of the organelle derived by optical diffraction analysis and the results of an ultrastructural cytochemical study designed to test whether the organelle contains nucleic acid.

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Prinz, William A. "Bridging the gap: Membrane contact sites in signaling, metabolism, and organelle dynamics." Journal of Cell Biology 205, no. 6 (June 23, 2014): 759–69. http://dx.doi.org/10.1083/jcb.201401126.

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Regions of close apposition between two organelles, often referred to as membrane contact sites (MCSs), mostly form between the endoplasmic reticulum and a second organelle, although contacts between mitochondria and other organelles have also begun to be characterized. Although these contact sites have been noted since cells first began to be visualized with electron microscopy, the functions of most of these domains long remained unclear. The last few years have witnessed a dramatic increase in our understanding of MCSs, revealing the critical roles they play in intracellular signaling, metabolism, the trafficking of metabolites, and organelle inheritance, division, and transport.

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Henne, W. Mike. "Organelle homeostasis principles: How organelle quality control and inter-organelle crosstalk promote cell survival." Developmental Cell 56, no. 7 (April 2021): 878–80. http://dx.doi.org/10.1016/j.devcel.2021.03.012.

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FOSTER, LEONARD J. "MASS SPECTROMETRY OUTGROWS SIMPLE BIOCHEMISTRY: NEW APPROACHES TO ORGANELLE PROTEOMICS." Biophysical Reviews and Letters 01, no. 02 (April 2006): 209–21. http://dx.doi.org/10.1142/s1793048006000057.

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Organelles are subcellular compartments or structures that typically carry out a defined set of functions within the cell. The functions of many organelles are known or predicted, but without knowing all the components of any recognized organelle it is difficult to fully understand them. Mass spectrometry-based proteomics now allows for routine identification of several hundreds or thousands of proteins in very complex samples; for cell biologists, organelles represent perhaps the most interesting class of cellular components to apply this new technology to. However, in order to analyze the proteome of an organelle it first must be purified, and the limitations in purifying any biological sample to homogeneity quickly become apparent to the vigilant mass spectrometrist. At the end of an organelle proteomic investigation, investigators are left with a long list of proteins whose location needs to be verified by an orthogonal method, a daunting prospect; or, they must accept an unknown and possibly very high level of incorrect localizations. Some of these caveats can be partially overcome by incorporating quantitative aspects into organelle proteomic studies. This review discusses some alternative approaches to organelle proteomics where questions of specificity and/or functional relevance are addressed by incorporating a quantitative dimension into the experiment.

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Hume, Alistair N., and Miguel C. Seabra. "Melanosomes on the move: a model to understand organelle dynamics." Biochemical Society Transactions 39, no. 5 (September 21, 2011): 1191–96. http://dx.doi.org/10.1042/bst0391191.

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Advances in live-cell microscopy have revealed the extraordinarily dynamic nature of intracellular organelles. Moreover, movement appears to be critical in establishing and maintaining intracellular organization and organellar and cellular function. Motility is regulated by the activity of organelle-associated motor proteins, kinesins, dyneins and myosins, which move cargo along polar MT (microtubule) and actin tracks. However, in most instances, the motors that move specific organelles remain mysterious. Over recent years, pigment granules, or melanosomes, within pigment cells have provided an excellent model for understanding the molecular mechanisms by which motor proteins associate with and move intracellular organelles. In the present paper, we discuss recent discoveries that shed light on the mechanisms of melanosome transport and highlight future prospects for the use of pigment cells in unravelling general molecular mechanisms of intracellular transport.

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Salogiannis, John, Martin J. Egan, and Samara L. Reck-Peterson. "Peroxisomes move by hitchhiking on early endosomes using the novel linker protein PxdA." Journal of Cell Biology 212, no. 3 (January 25, 2016): 289–96. http://dx.doi.org/10.1083/jcb.201512020.

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Eukaryotic cells use microtubule-based intracellular transport for the delivery of many subcellular cargos, including organelles. The canonical view of organelle transport is that organelles directly recruit molecular motors via cargo-specific adaptors. In contrast with this view, we show here that peroxisomes move by hitchhiking on early endosomes, an organelle that directly recruits the transport machinery. Using the filamentous fungus Aspergillus nidulans we found that hitchhiking is mediated by a novel endosome-associated linker protein, PxdA. PxdA is required for normal distribution and long-range movement of peroxisomes, but not early endosomes or nuclei. Using simultaneous time-lapse imaging, we find that early endosome-associated PxdA localizes to the leading edge of moving peroxisomes. We identify a coiled-coil region within PxdA that is necessary and sufficient for early endosome localization and peroxisome distribution and motility. These results present a new mechanism of microtubule-based organelle transport in which peroxisomes hitchhike on early endosomes and identify PxdA as the novel linker protein required for this coupling.

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Inagi, Reiko. "The Implication of Organelle Cross Talk in AKI." Nephron 144, no. 12 (2020): 634–37. http://dx.doi.org/10.1159/000508639.

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Organelle stress, such as mitochondrial or endoplasmic reticulum damage, plays a crucial role in the pathogenesis of acute kidney injury (AKI). Further, persistent organelle stress, which causes metabolic abnormality followed by inflammation and fibrosis, is an important mediator of AKI-to-CKD transition. Organelle stress closely links to the derangement of organelle cross talk. Organelles intricately interact with each other under the physiological conditions to maintain their function each other and subsequent cell fate. Organelle stress and their cross talk are now a focus of intensive researches in the field of AKI as they are in the field of CKD.

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Bretscher, Anthony. "Polarized growth and organelle segregation in yeast." Journal of Cell Biology 160, no. 6 (March 17, 2003): 811–16. http://dx.doi.org/10.1083/jcb.200301035.

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In yeast, growth and organelle segregation requires formin-dependent assembly of polarized actin cables. These tracks are used by myosin Vs to deliver secretory vesicles for cell growth, organelles for their segregation, and mRNA for fate determination. Several specific receptors have been identified that interact with the cargo-binding tails of the myosin Vs. A recent study implicates specific degradation in the bud of the vacuolar receptor, Vac17, as a mechanism for cell cycle–regulated segregation of this organelle.

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Morgan, Anthony J., Lianne C. Davis, Siegfried K. T. Y. Wagner, Alexander M. Lewis, John Parrington, Grant C. Churchill, and Antony Galione. "Bidirectional Ca2+ signaling occurs between the endoplasmic reticulum and acidic organelles." Journal of Cell Biology 200, no. 6 (March 11, 2013): 789–805. http://dx.doi.org/10.1083/jcb.201204078.

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The endoplasmic reticulum (ER) and acidic organelles (endo-lysosomes) act as separate Ca2+ stores that release Ca2+ in response to the second messengers IP3 and cADPR (ER) or NAADP (acidic organelles). Typically, trigger Ca2+ released from acidic organelles by NAADP subsequently recruits IP3 or ryanodine receptors on the ER, an anterograde signal important for amplification and Ca2+ oscillations/waves. We therefore investigated whether the ER can signal back to acidic organelles, using organelle pH as a reporter of NAADP action. We show that Ca2+ released from the ER can activate the NAADP pathway in two ways: first, by stimulating Ca2+-dependent NAADP synthesis; second, by activating NAADP-regulated channels. Moreover, the differential effects of EGTA and BAPTA (slow and fast Ca2+ chelators, respectively) suggest that the acidic organelles are preferentially activated by local microdomains of high Ca2+ at junctions between the ER and acidic organelles. Bidirectional organelle communication may have wider implications for endo-lysosomal function as well as the generation of Ca2+ oscillations and waves.

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Overly, C. C., H. I. Rieff, and P. J. Hollenbeck. "Organelle motility and metabolism in axons vs dendrites of cultured hippocampal neurons." Journal of Cell Science 109, no. 5 (May 1, 1996): 971–80. http://dx.doi.org/10.1242/jcs.109.5.971.

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Regional regulation of organelle transport seems likely to play an important role in establishing and maintaining distinct axonal and dendritic domains in neurons, and in managing differences in local metabolic demands. In addition, known differences in microtubule polarity and organization between axons and dendrites along with the directional selectivity of microtubule-based motor proteins suggest that patterns of organelle transport may differ in these two process types. To test this hypothesis, we compared the patterns of movement of different organelle classes in axons and different dendritic regions of cultured embryonic rat hippocampal neurons. We first examined the net direction of organelle transport in axons, proximal dendrites and distal dendrites by video-enhanced phase-contrast microscopy. We found significant regional variation in the net transport of large phase-dense vesicular organelles: they exhibited net retrograde transport in axons and distal dendrites, whereas they moved equally in both directions in proximal dendrites. No significant regional variation was found in the net transport of mitochondria or macropinosomes. Analysis of individual organelle motility revealed three additional differences in organelle transport between the two process types. First, in addition to the difference in net transport direction, the large phase-dense organelles exhibited more persistent changes in direction in proximal dendrites where microtubule polarity is mixed than in axons where microtubule polarity is uniform. Second, while the net direction of mitochondrial transport was similar in both processes, twice as many mitochondria were motile in axons than in dendrites. Third, the mean excursion length of moving mitochondria was significantly longer in axons than in dendrites. To determine whether there were regional differences in metabolic activity that might account for these motility differences, we labeled mitochondria with the vital dye, JC-1, which reveals differences in mitochondrial transmembrane potential. Staining of neurons with this dye revealed a greater proportion of highly charged, more metabolically active, mitochondria in dendrites than in axons. Together, our data reveal differences in organelle motility and metabolic properties in axons and dendrites of cultured hippocampal neurons.

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Ewenstein, B. M., M. J. Warhol, R. I. Handin, and J. S. Pober. "Composition of the von Willebrand factor storage organelle (Weibel-Palade body) isolated from cultured human umbilical vein endothelial cells." Journal of Cell Biology 104, no. 5 (May 1, 1987): 1423–33. http://dx.doi.org/10.1083/jcb.104.5.1423.

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von Willebrand factor (VWF) is a large, adhesive glycoprotein that is biosynthesized and secreted by cultured endothelial cells (EC). Although these cells constitutively release VWF, they also contain a storage pool of this protein that can be rapidly mobilized. In this study, a dense organelle fraction was isolated from cultured umbilical vein endothelial cells by centrifugation on a self-generated Percoll gradient. Stimulation of EC by 4-phorbol 12-myristate 13-acetate (PMA) resulted in the disappearance of this organelle fraction and the synchronous loss of Weibel-Palade bodies as judged by immunoelectron microscopy. Electrophoretic and serologic analyses of biosynthetically labeled dense organelle fraction revealed that it is comprised almost exclusively of VWF and its cleaved pro sequence. These two polypeptides were similarly localized exclusively to Weibel-Palade bodies by ultrastructural immunocytochemistry. The identity of the dense organelle as the Weibel-Palade body was further established by direct morphological examination of the dense organelle fraction. The VWF derived from this organelle is distributed among unusually high molecular weight multimers composed of fully processed monomeric subunits and is rapidly and quantitatively secreted in unmodified form after PMA stimulation. These studies: establish that the Weibel-Palade body is the endothelial-specific storage organelle for regulated VWF secretion; demonstrate that in cultured EC, the VWF concentrated in secretory organelles is of unusually high molecular weight and that this material may be rapidly mobilized in unmodified form; imply that proteolytic processing of VWF involved in regulated secretion takes place after translocation to the secretory organelle; provide a basis for further studies of intracellular protein trafficking in EC.

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Hasselbring, Benjamin M., and Duncan C. Krause. "Proteins P24 and P41 Function in the Regulation of Terminal-Organelle Development and Gliding Motility in Mycoplasma pneumoniae." Journal of Bacteriology 189, no. 20 (August 10, 2007): 7442–49. http://dx.doi.org/10.1128/jb.00867-07.

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ABSTRACT Mycoplasma pneumoniae is a major cause of bronchitis and atypical pneumonia in humans. This cell wall-less bacterium has a complex terminal organelle that functions in cytadherence and gliding motility. The gliding mechanism is unknown but is coordinated with terminal-organelle development during cell division. Disruption of M. pneumoniae open reading frame MPN311 results in loss of protein P41 and downstream gene product P24. P41 localizes to the base of the terminal organelle and is required to anchor the terminal organelle to the cell body, but during cell division, MPN311 insertion mutants also fail to properly regulate nascent terminal-organelle development spatially or gliding activity temporally. We measured gliding velocity and frequency and used fluorescent protein fusions and time-lapse imaging to assess the roles of P41 and P24 individually in terminal-organelle development and gliding function. P41 was necessary for normal gliding velocity and proper spatial positioning of new terminal organelles, while P24 was required for gliding frequency and new terminal-organelle formation at wild-type rates. However, P41 was essential for P24 function, and in the absence of P41, P24 exhibited a dynamic localization pattern. Finally, protein P28 requires P41 for stability, but analysis of a P28− mutant established that the MPN311 mutant phenotype was not a function of loss of P28.

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Schnapp, B. J., T. S. Reese, and R. Bechtold. "Kinesin is bound with high affinity to squid axon organelles that move to the plus-end of microtubules." Journal of Cell Biology 119, no. 2 (October 15, 1992): 389–99. http://dx.doi.org/10.1083/jcb.119.2.389.

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This paper addresses the question of whether microtubule-directed transport of vesicular organelles depends on the presence of a pool of cytosolic factors, including soluble motor proteins and accessory factors. Earlier studies with squid axon organelles (Schroer et al., 1988) suggested that the presence of cytosol induces a > 20-fold increase in the number of organelles moving per unit time on microtubules in vitro. These earlier studies, however, did not consider that cytosol might nonspecifically increase the numbers of moving organelles, i.e., by blocking adsorption of organelles to the coverglass. Here we report that treatment of the coverglass with casein, in the absence of cytosol, blocks adsorption of organelles to the coverglass and results in vigorous movement of vesicular organelles in the complete absence of soluble proteins. This technical improvement makes it possible, for the first time, to perform quantitative studies of organelle movement in the absence of cytosol. These new studies show that organelle movement activity (numbers of moving organelles/min/micron microtubule) of unextracted organelles is not increased by cytosol. Unextracted organelles move in single directions, approximately two thirds toward the plus-end and one third toward the minus-end of microtubules. Extraction of organelles with 600 mM KI completely inhibits minus-end, but not plus-end directed organelle movement. Upon addition of cytosol, minus-end directed movement of KI organelles is restored, while plus--end directed movement is unaffected. Biochemical studies indicate that KI-extracted organelles attach to microtubules in the presence of AMP-PNP and copurify with tightly bound kinesin. The bound kinesin is not extracted from organelles by 1 M KI, 1 M NaCl or carbonate (pH 11.3). These results suggest that kinesin is irreversibly bound to organelles that move to the plus-end of microtubules and that the presence of soluble kinesin and accessory factors is not required for movement of plus-end organelles in squid axons.

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31

Dove, A. "Cell-sorting technologies: Organelle recitals." Science 350, no. 6265 (December 3, 2015): 1267–69. http://dx.doi.org/10.1126/science.350.6265.1267.

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32

Bornens, Michel. "Organelle positioning and cell polarity." Nature Reviews Molecular Cell Biology 9, no. 11 (November 2008): 874–86. http://dx.doi.org/10.1038/nrm2524.

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Osteryoung, Katherine W., and Elizabeth Vierling. "Conserved cell and organelle division." Nature 376, no. 6540 (August 1995): 473–74. http://dx.doi.org/10.1038/376473b0.

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34

Luzio, J. P., B. A. Rous, N. A. Bright, P. R. Pryor, B. M. Mullock, and R. C. Piper. "Lysosome-endosome fusion and lysosome biogenesis." Journal of Cell Science 113, no. 9 (May 1, 2000): 1515–24. http://dx.doi.org/10.1242/jcs.113.9.1515.

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Recent data both from cell-free experiments and from cultured cells have shown that lysosomes can fuse directly with late endosomes to form a hybrid organelle. This has a led to a hypothesis that dense core lysosomes are in essence storage granules for acid hydrolases and that, when the former fuse with late endosomes, a hybrid organelle for digestion of endocytosed macromolecules is created. Lysosomes are then re-formed from hybrid organelles by a process involving condensation of contents. In this Commentary we review the evidence for formation of the hybrid organelles and discuss the current status of our understanding of the mechanisms of fusion and lysosome re-formation. We also review lysosome biosynthesis, showing how recent studies of lysosome-like organelles including the yeast vacuole, Drosophila eye pigment granules and mammalian secretory lysosomes have identified novel proteins involved in this process.

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Nakano, Akihiko, and Julia von Blume. "Organelle zones." Molecular Biology of the Cell 30, no. 6 (March 15, 2019): 731. http://dx.doi.org/10.1091/mbc.e18-12-0818.

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36

Fan, Jie, Haokang Zhang, Tasnif Rahman, Diana N. Stanton, and Leo Q. Wan. "Cell organelle-based analysis of cell chirality." Communicative & Integrative Biology 12, no. 1 (January 1, 2019): 78–81. http://dx.doi.org/10.1080/19420889.2019.1605277.

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37

Wells, William A. "An organelle knockout." Journal of Cell Biology 154, no. 5 (August 27, 2001): 904–5. http://dx.doi.org/10.1083/jcb1545rr2.

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38

Leslie, Mitch. "Tagging an organelle." Journal of Cell Biology 171, no. 2 (October 24, 2005): 195. http://dx.doi.org/10.1083/jcb1712fta2.

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39

Mai, Zhiming, Sudip Ghosh, Marta Frisardi, Ben Rosenthal, Rick Rogers, and John Samuelson. "Hsp60 Is Targeted to a Cryptic Mitochondrion-Derived Organelle (“Crypton”) in the Microaerophilic Protozoan Parasite Entamoeba histolytica." Molecular and Cellular Biology 19, no. 3 (March 1, 1999): 2198–205. http://dx.doi.org/10.1128/mcb.19.3.2198.

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ABSTRACT Entamoeba histolytica is a microaerophilic protozoan parasite in which neither mitochondria nor mitochondrion-derived organelles have been previously observed. Recently, a segment of anE. histolytica gene was identified that encoded a protein similar to the mitochondrial 60-kDa heat shock protein (Hsp60 or chaperonin 60), which refolds nuclear-encoded proteins after passage through organellar membranes. The possible function and localization of the amebic Hsp60 were explored here. Like Hsp60 of mitochondria, amebic Hsp60 RNA and protein were both strongly induced by incubating parasites at 42°C. 5′ and 3′ rapid amplifications of cDNA ends were used to obtain the entire E. histolytica hsp60 coding region, which predicted a 536-amino-acid Hsp60. The E. histolytica hsp60 gene protected from heat shockEscherichia coli groEL mutants, demonstrating the chaperonin function of the amebic Hsp60. The E. histolyticaHsp60, which lacked characteristic carboxy-terminal Gly-Met repeats, had a 21-amino-acid amino-terminal, organelle-targeting presequence that was cleaved in vivo. This presequence was necessary to target Hsp60 to one (and occasionally two or three) short, cylindrical organelle(s). In contrast, amebic alcohol dehydrogenase 1 and ferredoxin, which are bacteria-like enzymes, were diffusely distributed throughout the cytosol. We suggest that the Hsp60-associated, mitochondrion-derived organelle identified here be named “crypton,” as its structure was previously hidden and its function is still cryptic.

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Dvorak, Ann M., and Dian Feng. "The Vesiculo–Vacuolar Organelle (VVO): A New Endothelial Cell Permeability Organelle." Journal of Histochemistry & Cytochemistry 49, no. 4 (April 2001): 419–31. http://dx.doi.org/10.1177/002215540104900401.

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41

Marshall, Wallace F. "Organelle size control systems: From cell geometry to organelle-directed medicine." BioEssays 34, no. 9 (July 4, 2012): 721–24. http://dx.doi.org/10.1002/bies.201200043.

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42

Grant, Carly R., Juan Wan, and Arash Komeili. "Organelle Formation in Bacteria and Archaea." Annual Review of Cell and Developmental Biology 34, no. 1 (October 6, 2018): 217–38. http://dx.doi.org/10.1146/annurev-cellbio-100616-060908.

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Uncovering the mechanisms that underlie the biogenesis and maintenance of eukaryotic organelles is a vibrant and essential area of biological research. In comparison, little attention has been paid to the process of compartmentalization in bacteria and archaea. This lack of attention is in part due to the common misconception that organelles are a unique evolutionary invention of the “complex” eukaryotic cell and are absent from the “primitive” bacterial and archaeal cells. Comparisons across the tree of life are further complicated by the nebulous criteria used to designate subcellular structures as organelles. Here, with the aid of a unified definition of a membrane-bounded organelle, we present some of the recent findings in the study of lipid-bounded organelles in bacteria and archaea.

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43

Ahmad, Niaz, and Brent L. Nielsen. "Plant Organelle DNA Maintenance." Plants 9, no. 6 (May 28, 2020): 683. http://dx.doi.org/10.3390/plants9060683.

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Plant cells contain two double membrane bound organelles, plastids and mitochondria, that contain their own genomes. There is a very large variation in the sizes of mitochondrial genomes in higher plants, while the plastid genome remains relatively uniform across different species. One of the curious features of the organelle DNA is that it exists in a high copy number per mitochondria or chloroplast, which varies greatly in different tissues during plant development. The variations in copy number, morphology and genomic content reflect the diversity in organelle functions. The link between the metabolic needs of a cell and the capacity of mitochondria and chloroplasts to fulfill this demand is thought to act as a selective force on the number of organelles and genome copies per organelle. However, it is not yet clear how the activities of mitochondria and chloroplasts are coordinated in response to cellular and environmental cues. The relationship between genome copy number variation and the mechanism(s) by which the genomes are maintained through different developmental stages are yet to be fully understood. This Special Issue has several contributions that address current knowledge of higher plant organelle DNA. Here we briefly introduce these articles that discuss the importance of different aspects of the organelle genome in higher plants.

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Kimura, Kenji, and Akatsuki Kimura. "Intracellular organelles mediate cytoplasmic pulling force for centrosome centration in the Caenorhabditis elegans early embryo." Proceedings of the National Academy of Sciences 108, no. 1 (December 20, 2010): 137–42. http://dx.doi.org/10.1073/pnas.1013275108.

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The centrosome is generally maintained at the center of the cell. In animal cells, centrosome centration is powered by the pulling force of microtubules, which is dependent on cytoplasmic dynein. However, it is unclear how dynein brings the centrosome to the cell center, i.e., which structure inside the cell functions as a substrate to anchor dynein. Here, we provide evidence that a population of dynein, which is located on intracellular organelles and is responsible for organelle transport toward the centrosome, generates the force required for centrosome centration in Caenorhabditis elegans embryos. By using the database of full-genome RNAi in C. elegans, we identified dyrb-1, a dynein light chain subunit, as a potential subunit involved in dynein anchoring for centrosome centration. DYRB-1 is required for organelle movement toward the minus end of the microtubules. The temporal correlation between centrosome centration and the net movement of organelle transport was found to be significant. Centrosome centration was impaired when Rab7 and RILP, which mediate the association between organelles and dynein in mammalian cells, were knocked down. These results indicate that minus end-directed transport of intracellular organelles along the microtubules is required for centrosome centration in C. elegans embryos. On the basis of this finding, we propose a model in which the reaction forces of organelle transport generated along microtubules act as a driving force that pulls the centrosomes toward the cell center. This is the first model, to our knowledge, providing a mechanical basis for cytoplasmic pulling force for centrosome centration.

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Klemm, Robin W. "Getting in Touch Is an Important Step: Control of Metabolism at Organelle Contact Sites." Contact 4 (January 2021): 251525642199370. http://dx.doi.org/10.1177/2515256421993708.

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Metabolic pathways are often spread over several organelles and need to be functionally integrated by controlled organelle communication. Physical organelle contact-sites have emerged as critical hubs in the regulation of cellular metabolism, but the molecular understanding of mechanisms that mediate formation or regulation of organelle interfaces was until recently relatively limited. Mitochondria are central organelles in anabolic and catabolic pathways and therefore interact with a number of other cellular compartments including the endoplasmic reticulum (ER) and lipid droplets (LDs). An interesting set of recent work has shed new light on the molecular basis forming these contact sites. This brief overview describes the discovery of unanticipated functions of contact sites between the ER, mitochondria and LDs in de novo synthesis of storage lipids of brown and white adipocytes. Interestingly, the factors involved in mediating the interaction between these organelles are subject to unexpected modes of regulation through newly uncovered Phospho-FFAT motifs. These results suggest dynamic regulation of contact sites between organelles and indicate that spatial organization of organelles within the cell contributes to the control of metabolism.

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46

Serrano-Puebla, Ana, and Patricia Boya. "Lysosomal membrane permeabilization as a cell death mechanism in cancer cells." Biochemical Society Transactions 46, no. 2 (February 22, 2018): 207–15. http://dx.doi.org/10.1042/bst20170130.

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Lysosomes are acidic organelles that contain hydrolytic enzymes that mediate the intracellular degradation of macromolecules. Damage of these organelles often results in lysosomal membrane permeabilization (LMP) and the release into the cytoplasm of the soluble lysosomal contents, which include proteolytic enzymes of the cathepsin family. This, in turn, activates several intracellular cascades that promote a type of regulated cell death, called lysosome-dependent cell death (LDCD). LDCD can be inhibited by pharmacological or genetic blockade of cathepsin activity, or by protecting the lysosomal membrane, thereby stabilizing the organelle. Lysosomal alterations are common in cancer cells and may increase the sensitivity of these cells to agents that promote LMP. In this review, we summarize recent findings supporting the use of LDCD as a means of killing cancer cells.

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47

Ci, Yali, and Lei Shi. "Compartmentalized replication organelle of flavivirus at the ER and the factors involved." Cellular and Molecular Life Sciences 78, no. 11 (April 12, 2021): 4939–54. http://dx.doi.org/10.1007/s00018-021-03834-6.

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AbstractFlaviviruses are positive-sense single-stranded RNA viruses that pose a considerable threat to human health. Flaviviruses replicate in compartmentalized replication organelles derived from the host endoplasmic reticulum (ER). The characteristic architecture of flavivirus replication organelles includes invaginated vesicle packets and convoluted membrane structures. Multiple factors, including both viral proteins and host factors, contribute to the biogenesis of the flavivirus replication organelle. Several viral nonstructural (NS) proteins with membrane activity induce ER rearrangement to build replication compartments, and other NS proteins constitute the replication complexes (RC) in the compartments. Host protein and lipid factors facilitate the formation of replication organelles. The lipid membrane, proteins and viral RNA together form the functional compartmentalized replication organelle, in which the flaviviruses efficiently synthesize viral RNA. Here, we reviewed recent advances in understanding the structure and biogenesis of flavivirus replication organelles, and we further discuss the function of virus NS proteins and related host factors as well as their roles in building the replication organelle.

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Sasaki, Kanae, and Hiderou Yoshida. "Organelle Zones." Cell Structure and Function 44, no. 2 (2019): 85–94. http://dx.doi.org/10.1247/csf.19010.

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Liu, Fangfang, Seng Kah Ng, Yanfen Lu, Wilson Low, Julian Lai, and Gregory Jedd. "Making two organelles from one: Woronin body biogenesis by peroxisomal protein sorting." Journal of Cell Biology 180, no. 2 (January 28, 2008): 325–39. http://dx.doi.org/10.1083/jcb.200705049.

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Woronin bodies (WBs) are dense-core organelles that are found exclusively in filamentous fungi and that seal the septal pore in response to wounding. These organelles consist of a membrane-bound protein matrix comprised of the HEX protein and, although they form from peroxisomes, their biogenesis is poorly understood. In Neurospora crassa, we identify Woronin sorting complex (WSC), a PMP22/MPV17-related membrane protein with dual functions in WB biogenesis. WSC localizes to large peroxisome membranes where it self-assembles into detergent-resistant oligomers that envelop HEX assemblies, producing asymmetrical nascent WBs. In a reaction requiring WSC, these structures are delivered to the cell cortex, which permits partitioning of the nascent WB and WB inheritance. Our findings suggest that WSC and HEX collaborate and control distinct aspects of WB biogenesis and that cortical association depends on WSC, which in turn depends on HEX. This dependency helps order events across the organellar membrane, permitting the peroxisome to produce a second organelle with a distinct composition and intracellular distribution.

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50

Pickett, James. "Organelle blueprints unveiled." Nature Reviews Molecular Cell Biology 8, no. 1 (January 2007): 2. http://dx.doi.org/10.1038/nrm2089.

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Journal articles on the topic 'Cell organelle'

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