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Artykuły w czasopismach na temat „Secretory compartments”

Autor: Grafiati

Data publikacji: 19 października 2024

Data aktualizacji: 31 lipca 2025

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1

Schmidt, W. K., and H. P. Moore. "Ionic milieu controls the compartment-specific activation of pro-opiomelanocortin processing in AtT-20 cells." Molecular Biology of the Cell 6, no. 10 (1995): 1271–85. http://dx.doi.org/10.1091/mbc.6.10.1271.

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Newly synthesized prohormones and their processing enzymes transit through the same compartments before being packaged into regulated secretory granules. Despite this coordinated intracellular transport, prohormone processing does not occur until late in the secretory pathway. In the mouse pituitary AtT-20 cell line, conversion of pro-opiomelanocortin (POMC) to mature adrenocorticotropic hormone involves the prohormone convertase PC1. The mechanism by which this proteolytic processing is restricted to late secretory compartments is unknown; PC1 activity could be regulated by compartment-specif

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2

Derré, Isabelle, and Ralph R. Isberg. "LidA, a Translocated Substrate of the Legionella pneumophila Type IV Secretion System, Interferes with the Early Secretory Pathway." Infection and Immunity 73, no. 7 (2005): 4370–80. http://dx.doi.org/10.1128/iai.73.7.4370-4380.2005.

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ABSTRACT Legionella pneumophila uses a type IV secretion system to deliver effector molecules into the host cell and establish its replication vacuole. In this study, we investigated the role of LidA, a translocated substrate associated with the surface of the L. pneumophila-containing vacuole. LidA is secreted into the host cell throughout the replication cycle of the bacteria and associates with compartments of the early secretory pathway. When overexpressed in mammalian cells or yeast, LidA interferes with the early secretory pathway, probably via a domain predicted to be rich in coiled-coi

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Bianco, P., M. Riminucci, E. Bonucci, J. D. Termine, and P. G. Robey. "Bone sialoprotein (BSP) secretion and osteoblast differentiation: relationship to bromodeoxyuridine incorporation, alkaline phosphatase, and matrix deposition." Journal of Histochemistry & Cytochemistry 41, no. 2 (1993): 183–91. http://dx.doi.org/10.1177/41.2.8419458.

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We defined two distinct maturational compartments (proliferative and secretory) of osteogenic cells in vivo on the basis of ALP activity, BrdU incorporation, cell shape, and BSP production. BSP immunoreactivity was found to mark cells in the secretory but not in the proliferative compartment. We established the phenotypic similarity of primitive marrow stromal cells with proliferating perichondral cells (fibroblast-like, ALP+, BrdU+, BSP-). This suggests the potential functional equivalence of the two cell types as committed non-secretory osteogenic cells and points to the duality of osteogeni

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4

Tobin, V. A., and M. Ludwig. "The actin filament and dendritic peptide release." Biochemical Society Transactions 35, no. 5 (2007): 1243–46. http://dx.doi.org/10.1042/bst0351243.

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F-actin remodelling has been implicated in regulated secretion from many cell types, in particular secretion from neuron axon terminals and neuroendocrine cell types. Cortical F-actin has long been postulated to act as a barrier to vesicle movement and hence to inhibit secretion; however, more recent studies point to F-actin remodelling providing both supporting and restraining roles in secretion. Magnocellular neurons of the supraoptic nucleus secrete either oxytocin or vasopressin from their dendrites as well as their axon terminals; and peptide release from these two compartments can be dif

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5

Naik, Haley B., Melissa Beshire, Breda M. Walsh, Jingjing Liu, and David I. Soybel. "Secretory state regulates Zn2+ transport in gastric parietal cell of the rabbit." American Journal of Physiology-Cell Physiology 297, no. 4 (2009): C979—C989. http://dx.doi.org/10.1152/ajpcell.00577.2008.

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Secretory compartments of neurons, endocrine cells, and exocrine glands are acidic and contain high levels of labile Zn2+. Previously, we reported evidence that acidity is regulated, in part, by the content of Zn2+ in the secretory [i.e., tubulovesicle (TV)] compartment of the acid-secreting gastric parietal cell. Here we report studies focusing on the mechanisms of Zn2+ transport by the TV compartment in the mammalian (rabbit) gastric parietal cell. Uptake of Zn2+ by isolated TV structures was monitored with a novel application of the fluorescent Zn2+ reporter N-(6-methoxy-8-quinolyl)- para-t

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6

Plutner, H., A. D. Cox, S. Pind, et al. "Rab1b regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments." Journal of Cell Biology 115, no. 1 (1991): 31–43. http://dx.doi.org/10.1083/jcb.115.1.31.

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We report an essential role for the ras-related small GTP-binding protein rab1b in vesicular transport in mammalian cells. mAbs detect rab1b in both the ER and Golgi compartments. Using an assay which reconstitutes transport between the ER and the cis-Golgi compartment, we find that rab1b is required during an initial step in export of protein from the ER. In addition, it is also required for transport of protein between successive cis- and medial-Golgi compartments. We suggest that rab1b may provide a common link between upstream and downstream components of the vesicular fission and fusion m

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7

Raote, Ishier, and Vivek Malhotra. "Protein transport by vesicles and tunnels." Journal of Cell Biology 218, no. 3 (2019): 737–39. http://dx.doi.org/10.1083/jcb.201811073.

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Palade’s corpus placed small vesicles as the sole means to transport proteins across stable distinct compartments of the secretory pathway. We suggest that cargo, spatial organization of secretory compartments, and the timing of fission of cargo-filled containers dictate the design of transport intermediates that can be vesicles and transient direct tunnels.

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8

Oyarce, A. M., and B. A. Eipper. "Identification of subcellular compartments containing peptidylglycine alpha-amidating monooxygenase in rat anterior pituitary." Journal of Cell Science 108, no. 1 (1995): 287–97. http://dx.doi.org/10.1242/jcs.108.1.287.

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Both soluble and integral membrane forms of peptidylglycine alpha-amidating monooxygenase (PAM) are expressed in the rat anterior pituitary, making it an ideal model system for studying the routing of proteins into secretory granules. To identify the subcellular compartments involved in the routing of integral membrane PAM, we used subcellular fractionation, metabolic labeling and immunoblot analysis. Mature secretory granules were found to contain full-length integral membrane PAM along with a significant amount of soluble PAM generated by endoproteolytic cleavage. PAM proteins were not co-di

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9

Diekwisch, Thomas G. H. "Subunit Compartments of Secretory Stage Enamel Matrix." Connective Tissue Research 38, no. 1-4 (1998): 101–11. http://dx.doi.org/10.3109/03008209809017026.

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10

Saraste, Jaakko. "Introduction: Enigmatic compartments of the secretory pathway." Seminars in Cell Biology 3, no. 5 (1992): 299. http://dx.doi.org/10.1016/1043-4682(92)90016-o.

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11

Messenger, Scott W., Diana D. H. Thomas, Michelle A. Falkowski, Jennifer A. Byrne, Fred S. Gorelick, and Guy E. Groblewski. "Tumor protein D52 controls trafficking of an apical endolysosomal secretory pathway in pancreatic acinar cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 305, no. 6 (2013): G439—G452. http://dx.doi.org/10.1152/ajpgi.00143.2013.

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Zymogen granule (ZG) formation in acinar cells involves zymogen cargo sorting from trans-Golgi into immature secretory granules (ISGs). ISG maturation progresses by removal of lysosomal membrane and select content proteins, which enter endosomal intermediates prior to their apical exocytosis. Constitutive and stimulated secretion through this mechanism is termed the constitutive-like and minor-regulated pathways, respectively. However, the molecular components that control membrane trafficking within these endosomal compartments are largely unknown. We show that tumor protein D52 is highly exp

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12

Wassmer, Thomas, Roland Kissmehl, Jean Cohen, and Helmut Plattner. "Seventeen a-Subunit Isoforms of Paramecium V-ATPase Provide High Specialization in Localization and Function." Molecular Biology of the Cell 17, no. 2 (2006): 917–30. http://dx.doi.org/10.1091/mbc.e05-06-0511.

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In the Paramecium tetraurelia genome, 17 genes encoding the 100-kDa-subunit (a-subunit) of the vacuolar-proton-ATPase were identified, representing by far the largest number of a-subunit genes encountered in any organism investigated so far. They group into nine clusters, eight pairs with >82% amino acid identity and one single gene. Green fluorescent protein-tagging of representatives of the nine clusters revealed highly specific targeting to at least seven different compartments, among them dense core secretory vesicles (trichocysts), the contractile vacuole complex, and phagosomes. RNA i

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13

Raposo, Graça, Danielle Tenza, Salahedine Mecheri, Roger Peronet, Christian Bonnerot, and Catherine Desaymard. "Accumulation of Major Histocompatibility Complex Class II Molecules in Mast Cell Secretory Granules and Their Release upon Degranulation." Molecular Biology of the Cell 8, no. 12 (1997): 2631–45. http://dx.doi.org/10.1091/mbc.8.12.2631.

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To investigate the relationship between major histocompatibility complex (MHC) class II compartments, secretory granules, and secretory lysosomes, we analyzed the localization and fate of MHC class II molecules in mast cells. In bone marrow-derived mast cells, the bulk of MHC class II molecules is contained in two distinct compartments, with features of both lysosomal compartments and secretory granules defined by their protein content and their accessibility to endocytic tracers. Type I granules display internal membrane vesicles and are accessed by exogenous molecules after a time lag of 20

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14

Graham, T. R., and S. D. Emr. "Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant." Journal of Cell Biology 114, no. 2 (1991): 207–18. http://dx.doi.org/10.1083/jcb.114.2.207.

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The sec18 and sec23 secretory mutants of Saccharomyces cerevisiae have previously been shown to exhibit temperature-conditional defects in protein transport from the ER to the Golgi complex (Novick, P., S. Ferro, and R. Schekman, 1981. Cell. 25:461-469). We have found that the Sec18 and Sec23 protein functions are rapidly inactivated upon shifting mutant cells to the nonpermissive temperature (less than 1 min). This has permitted an analysis of the potential role these SEC gene products play in transport events distal to the ER. The sec-dependent transport of alpha-factor (alpha f) and carboxy

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15

Kobayashi, T., and J. M. Robinson. "A novel intracellular compartment with unusual secretory properties in human neutrophils." Journal of Cell Biology 113, no. 4 (1991): 743–56. http://dx.doi.org/10.1083/jcb.113.4.743.

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Human neutrophils contain a novel intracellular compartment that is distinct from the previously characterized azurophil and specific granules. This compartment is distinguished by the presence of cytochemically detectable alkaline phosphatase activity. The alkaline phosphatase-containing compartments are short rod-shaped organelles that rapidly undergo a dramatic reorganization upon cell stimulation with either a chemoattractant or an active phorbol ester. Biochemical analysis shows that in unstimulated neutrophils the majority of the alkaline phosphatase activity is intracellular, but after

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16

Laulagnier, Karine, Nicole L. Schieber, Tanja Maritzen, Volker Haucke, Robert G. Parton, and Jean Gruenberg. "Role of AP1 and Gadkin in the traffic of secretory endo-lysosomes." Molecular Biology of the Cell 22, no. 12 (2011): 2068–82. http://dx.doi.org/10.1091/mbc.e11-03-0193.

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Whereas lysosome-related organelles (LRO) of specialized cells display both exocytic and endocytic features, lysosomes in nonspecialized cells can also acquire the property to fuse with the plasma membrane upon an acute rise in cytosolic calcium. Here, we characterize this unconventional secretory pathway in fibroblast-like cells, by monitoring the appearance of Lamp1 on the plasma membrane and the release of lysosomal enzymes into the medium. After sequential ablation of endocytic compartments in living cells, we find that donor membranes primarily derive from a late compartment, but that an

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17

Orci, L., M. Ravazzola, M. Amherdt, et al. "Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles." Journal of Cell Biology 103, no. 6 (1986): 2273–81. http://dx.doi.org/10.1083/jcb.103.6.2273.

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Proinsulin is a single polypeptide chain composed of the B and A subunits of insulin joined by the C-peptide region. Proinsulin is converted to insulin during the maturation of secretory vesicles by the action of two proteases and conversion is inhibited by ionophores that disrupted intracellular H+ gradients. To determine if conversion of prohormone to hormone actually occurs in an acidic secretory vesicle, cultured rat islet cells were incubated in the presence of 3-(2,4-dinitroanilino)-3' amino-N-methyldipropylamine (DAMP), a basic congener of dinitrophenol that concentrates in acidic compa

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18

Bogan, Jonathan S., and Harvey F. Lodish. "Two Compartments for Insulin-Stimulated Exocytosis in 3t3-L1 Adipocytes Defined by Endogenous Acrp30 and Glut4." Journal of Cell Biology 146, no. 3 (1999): 609–20. http://dx.doi.org/10.1083/jcb.146.3.609.

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Insulin stimulates adipose cells both to secrete proteins and to translocate the GLUT4 glucose transporter from an intracellular compartment to the plasma membrane. We demonstrate that whereas insulin stimulation of 3T3-L1 adipocytes has no effect on secretion of the α3 chain of type VI collagen, secretion of the protein hormone adipocyte complement related protein of 30 kD (ACRP30) is markedly enhanced. Like GLUT4, regulated exocytosis of ACRP30 appears to require phosphatidylinositol-3-kinase activity, since insulin-stimulated ACRP30 secretion is blocked by pharmacologic inhibitors of this e

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19

Vellosillo, Tamara, José R. Dinneny, Chris R. Somerville, and David W. Ehrhardt. "TRANVIA (TVA) facilitates cellulose synthase trafficking and delivery to the plasma membrane." Proceedings of the National Academy of Sciences 118, no. 30 (2021): e2021790118. http://dx.doi.org/10.1073/pnas.2021790118.

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Cellulose is synthesized at the plasma membrane by cellulose synthase (CESA) complexes (CSCs), which are assembled in the Golgi and secreted to the plasma membrane through the trans-Golgi network (TGN) compartment. However, the molecular mechanisms that guide CSCs through the secretory system and deliver them to the plasma membrane are poorly understood. Here, we identified an uncharacterized gene, TRANVIA (TVA), that is transcriptionally coregulated with the CESA genes required for primary cell wall synthesis. The tva mutant exhibits enhanced sensitivity to cellulose synthesis inhibitors; red

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20

Stephens, Samuel B., and Christopher V. Nicchitta. "Divergent Regulation of Protein Synthesis in the Cytosol and Endoplasmic Reticulum Compartments of Mammalian Cells." Molecular Biology of the Cell 19, no. 2 (2008): 623–32. http://dx.doi.org/10.1091/mbc.e07-07-0677.

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In eukaryotic cells, mRNAs encoding signal sequence-bearing proteins undergo translation-dependent trafficking to the endoplasmic reticulum (ER), thereby restricting secretory and integral membrane protein synthesis to the ER compartment. However, recent studies demonstrating that mRNAs encoding cytosolic/nucleoplasmic proteins are represented on ER-bound polyribosomes suggest a global role for the ER in cellular protein synthesis. Here, we examined the steady-state protein synthesis rates and compartmental distribution of newly synthesized proteins in the cytosol and ER compartments. We repor

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21

McCaffrey, Kathleen, and Ineke Braakman. "Protein quality control at the endoplasmic reticulum." Essays in Biochemistry 60, no. 2 (2016): 227–35. http://dx.doi.org/10.1042/ebc20160003.

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The ER (endoplasmic reticulum) is the protein folding ‘factory’ of the secretory pathway. Virtually all proteins destined for the plasma membrane, the extracellular space or other secretory compartments undergo folding and maturation within the ER. The ER hosts a unique PQC (protein quality control) system that allows specialized modifications such as glycosylation and disulfide bond formation essential for the correct folding and function of many secretory proteins. It is also the major checkpoint for misfolded or aggregation-prone proteins that may be toxic to the cell or extracellular envir

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22

Trifaró, J. M. "Scinderin and cortical F-actin are components of the secretory machinery." Canadian Journal of Physiology and Pharmacology 77, no. 9 (1999): 660–71. http://dx.doi.org/10.1139/y99-074.

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Secretory vesicle exocytosis is the mechanism of release of neurotransmitters and neuropeptides. Secretory vesicles are localized in at least two morphologically and functionally distinct compartments: the reserve pool and the release-ready pool. Filamentous actin networks play an important role in this compartmentalization and in the trafficking of vesicles between these compartments. The cortical F-actin network constitutes a barrier (negative clamp) to the movement of secretory vesicles to release sites, and it must be locally disassembled to allow translocation of secretory vesicles in pre

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Suzuki, Eisuke, Namino Ogawa, Taka-aki Takeda, et al. "Detailed analyses of the crucial functions of Zn transporter proteins in alkaline phosphatase activation." Journal of Biological Chemistry 295, no. 17 (2020): 5669–84. http://dx.doi.org/10.1074/jbc.ra120.012610.

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Numerous zinc ectoenzymes are metalated by zinc and activated in the compartments of the early secretory pathway before reaching their destination. Zn transporter (ZNT) proteins located in these compartments are essential for ectoenzyme activation. We have previously reported that ZNT proteins, specifically ZNT5–ZNT6 heterodimers and ZNT7 homodimers, play critical roles in the activation of zinc ectoenzymes, such as alkaline phosphatases (ALPs), by mobilizing cytosolic zinc into these compartments. However, this process remains incompletely understood. Here, using genetically-engineered chicke

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24

Jost, Carolina, Lloyd Klickstein, Erica Wetzler, Anoopa Kumar, and Melvin Berger. "Intracellular Storage and Regulated Plasma Membrane Expression of Human Complement Receptor Type 1 in Rat Basophil Leukemia Cell Transfectants." Blood 92, no. 1 (1998): 300–309. http://dx.doi.org/10.1182/blood.v92.1.300.413k29_300_309.

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Polymorphonuclear neutrophils (PMN) contain multiple distinct secretory compartments that are sequentially mobilized during cell activation. Complement receptor type 1 (CR1) is a marker for a readily mobilizable secretory vesicle compartment, which can undergo exocytic fusion with the plasma membrane independently of secretion of traditional granule contents. The basis for the formation of these distinct compartments is incompletely understood. Primary and secondary granules are generated directly from the Golgi complex during different stages of development of the cell, obviating the need for

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Meagher, James, René Zellweger, and Luis Filgueira. "Functional Dissociation of the Basolateral Transcytotic Compartment from the Apical Phago-lysosomal Compartment in Human Osteoclasts." Journal of Histochemistry & Cytochemistry 53, no. 5 (2005): 665–70. http://dx.doi.org/10.1369/jhc.4a6476.2005.

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Tartrate-resistant acid phosphatase (TRAP) is essential for elimination of Staphylococcus aureus, the main infectious agent responsible for osteomyelitis. This in vitro study investigated uptake and processing of fluorescence-labeled S. aureus by human osteoclasts and dendritic cells. The cells were stained for TRAP and the acidic compartment using a fluorescence-based protocol. In dendritic cells, TRAP and bacteria were colocalized. In osteoclasts, there was no colocalization of bacteria, TRAP, or the acidic compartment, indicating that there are three distinct vesicular compartments: the api

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Glasser, S. R., J. Julian, G. L. Decker, J. P. Tang, and D. D. Carson. "Development of morphological and functional polarity in primary cultures of immature rat uterine epithelial cells." Journal of Cell Biology 107, no. 6 (1988): 2409–23. http://dx.doi.org/10.1083/jcb.107.6.2409.

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The present study describes a culture environment in which luminal epithelial cells isolated from immature rat uteri and cultured on a matrix-coated permeable surface, with separate apical and basal secretory compartments, proliferate to confluence. Subsequently the cells undergo a process of differentiation accompanied by progressive development of functional polarity. Ultrastructural and immunocytochemical evidence verifies the ability of these primary cultures to regain polar organization, separate membrane domains, and form functional tight junctions as demonstrated by the development of t

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Styers, Melanie L., Amber K. O'Connor, Robert Grabski, Estelle Cormet-Boyaka та Elizabeth Sztul. "Depletion of β-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1". American Journal of Physiology-Cell Physiology 294, № 6 (2008): C1485—C1498. http://dx.doi.org/10.1152/ajpcell.00010.2008.

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We have utilized small interfering RNA (siRNA)-mediated depletion of the β-COP subunit of COP-I to explore COP-I function in organellar compartmentalization and protein traffic. Reduction in β-COP levels causes the colocalization of markers for the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN), and recycling endosomes in large, globular compartments. The lack of spatial differentiation of these compartments is not due to a general collapse of all cellular organelles since markers for the early endosomes and lysosomes do not redistribute to

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Sengeløv, H., L. Kjeldsen, and N. Borregaard. "Control of exocytosis in early neutrophil activation." Journal of Immunology 150, no. 4 (1993): 1535–43. http://dx.doi.org/10.4049/jimmunol.150.4.1535.

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Abstract Exocytosis of human neutrophil secretory vesicles, gelatinase granules, specific granules, and azurophil granules was measured during modulation of the intracellular free calcium concentration. A strict rank order of exocytosis of the four compartments was observed when cytosolic calcium was elevated by an ionophore in Fura-2-loaded cells. The rank order was: secretory vesicles, gelatinase granules, specific granules, and azurophil granules. Secretory vesicles were exceptionally sensitive to cytosolic free calcium, being completely mobilized after small cytosolic calcium transients. K

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Pakdel, Mehrshad, and Julia von Blume. "Exploring new routes for secretory protein export from the trans-Golgi network." Molecular Biology of the Cell 29, no. 3 (2018): 235–40. http://dx.doi.org/10.1091/mbc.e17-02-0117.

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Sorting of soluble proteins for transport to intracellular compartments and for secretion from cells is essential for cell and tissue homeostasis. The trans-Golgi network (TGN) is a major sorting station that sorts secretory proteins into specific carriers to transport them to their final destinations. The sorting of lysosomal hydrolases at the TGN by the mannose 6-phosphate receptor is well understood. The recent discovery of a Ca2+-based sorting of secretory cargo at the TGN is beginning to uncover the mechanism by which cells sort secretory cargoes from Golgi residents and cargoes destined

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Slot, Jan W., Gabriella Garruti, Sally Martin, et al. "Glucose Transporter (GLUT-4) Is Targeted to Secretory Granules in Rat Atrial Cardiomyocytes." Journal of Cell Biology 137, no. 6 (1997): 1243–54. http://dx.doi.org/10.1083/jcb.137.6.1243.

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The insulin-responsive glucose transporter GLUT-4 is found in muscle and fat cells in the transGolgi reticulum (TGR) and in an intracellular tubulovesicular compartment, from where it undergoes insulindependent movement to the cell surface. To examine the relationship between these GLUT-4–containing compartments and the regulated secretory pathway we have localized GLUT-4 in atrial cardiomyocytes. This cell type secretes an antihypertensive hormone, referred to as the atrial natriuretic factor (ANF), in response to elevated blood pressure. We show that GLUT-4 is targeted in the atrial cell to

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Anderson, Timothy J., Sally Martin, Jennifer L. Berka, David E. James, Jan W. Slot, and Jennifer L. Stow. "Distinct localization of renin and GLUT-4 in juxtaglomerular cells of mouse kidney." American Journal of Physiology-Renal Physiology 274, no. 1 (1998): F26—F33. http://dx.doi.org/10.1152/ajprenal.1998.274.1.f26.

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The insulin-responsive glucose transporter, GLUT-4, is found primarily in adipocytes and skeletal muscle cells, where it is sequestered in a specialized recycling compartment, from which it can be recruited to the cell surface following insulin stimulation. Lower levels of GLUT-4 are also expressed in other tissues, including the kidney, where it is present particularly in cells of the afferent arteriole and juxtaglomerular apparatus (JGA). The exact nature of GLUT-4-containing compartments and their relationship to other regulated trafficking pathways in different cells are not yet well defin

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Drouin, Arnaud, Rémi Favier, Jean-Marc Massé, et al. "Newly recognized cellular abnormalities in the gray platelet syndrome." Blood 98, no. 5 (2001): 1382–91. http://dx.doi.org/10.1182/blood.v98.5.1382.

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The gray platelet syndrome (GPS) is a rare congenital bleeding disorder in which thrombocytopenia is associated with increased platelet size and decreased α-granule content. This report describes 3 new pediatric cases presenting with the classical platelet abnormalities of GPS within one family with normal parents. Examination of blood smears of the 3 patients demonstrated not only gray platelets, but also gray polymorphonuclear neutrophils (PMNs) with decreased or abnormally distributed components of secretory compartments (alkaline phosphatase, CD35, CD11b/CD18). Secondary granules were also

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Gomez-Navarro, Natalia, and Elizabeth Miller. "Protein sorting at the ER–Golgi interface." Journal of Cell Biology 215, no. 6 (2016): 769–78. http://dx.doi.org/10.1083/jcb.201610031.

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Protein traffic is of critical importance for normal cellular physiology. In eukaryotes, spherical transport vesicles move proteins and lipids from one internal membrane-bound compartment to another within the secretory pathway. The process of directing each individual protein to a specific destination (known as protein sorting) is a crucial event that is intrinsically linked to vesicle biogenesis. In this review, we summarize the principles of cargo sorting by the vesicle traffic machinery and consider the diverse mechanisms by which cargo proteins are selected and captured into different tra

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Sanchez, Veronica, Elizabeth Sztul, and William J. Britt. "Human Cytomegalovirus pp28 (UL99) Localizes to a Cytoplasmic Compartment Which Overlaps the Endoplasmic Reticulum-Golgi-Intermediate Compartment." Journal of Virology 74, no. 8 (2000): 3842–51. http://dx.doi.org/10.1128/jvi.74.8.3842-3851.2000.

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ABSTRACT Although the assembly of herpesviruses has remained an active area of investigation, considerable controversy continues to surround the cellular location of tegument and envelope acquisition. This controversy is particularly evident when the proposed pathways for α- and β-herpesvirus assembly are compared. We have approached this aspect of human cytomegalovirus (HCMV) assembly, specifically, envelopment, by investigating the intracellular trafficking of viral tegument proteins which localize in the cytoplasms of infected cells. In this study we have demonstrated that the virion tegume

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Porter, Brad W., Christen Y. L. Yuen, and David A. Christopher. "Dual protein trafficking to secretory and non-secretory cell compartments: Clear or double vision?" Plant Science 234 (May 2015): 174–79. http://dx.doi.org/10.1016/j.plantsci.2015.02.013.

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Kreiner, T., and H. P. Moore. "Membrane traffic between secretory compartments is differentially affected during mitosis." Cell Regulation 1, no. 5 (1990): 415–24. http://dx.doi.org/10.1091/mbc.1.5.415.

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Membrane traffic has been shown to be regulated during cell division. In particular, with the use of viral membrane proteins as markers, endoplasmic reticulum (ER)-to-Golgi transport in mitotic cells has been shown to be essentially blocked. However, the effect of mitosis on other steps in the secretory pathway is less clear, because an early block makes examination of following steps difficult. Here, we report studies on the functional characteristics of secretory pathways in mitotic mammalian tissue culture cells by the use of a variety of markers. Chinese hamster ovary cells were transfecte

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Pfeffer, Suzanne R. "Rab GTPase localization and Rab cascades in Golgi transport." Biochemical Society Transactions 40, no. 6 (2012): 1373–77. http://dx.doi.org/10.1042/bst20120168.

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Rab GTPases are master regulators of membrane traffic. By binding to distinct sets of effector proteins, Rabs catalyse the formation of function-specifying membrane microdomains. They are delivered to membranes by a protein named GDI (guanine-nucleotide-dissociation inhibitor) and are stabilized there after nucleotide exchange by effector binding. In the present mini-review, I discuss what we know about how Rab GTPases are delivered to the correct membrane-bound compartments and how Rab GTPase cascades order Rabs within the secretory and endocytic pathways. Finally, I describe how Rab cascades

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Cruz-Garcia, David, Amy J. Curwin, Jean-François Popoff, Caroline Bruns, Juan M. Duran, and Vivek Malhotra. "Remodeling of secretory compartments creates CUPS during nutrient starvation." Journal of Cell Biology 207, no. 6 (2014): 695–703. http://dx.doi.org/10.1083/jcb.201407119.

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Upon starvation, Grh1, a peripheral membrane protein located at endoplasmic reticulum (ER) exit sites and early Golgi in Saccharomyces cerevisiae under growth conditions, relocates to a compartment called compartment for unconventional protein secretion (CUPS). Here we report that CUPS lack Golgi enzymes, but contain the coat protein complex II (COPII) vesicle tethering protein Uso1 and the Golgi t-SNARE Sed5. Interestingly, CUPS biogenesis is independent of COPII- and COPI-mediated membrane transport. Pik1- and Sec7-mediated membrane export from the late Golgi is required for complete assembl

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Sallese, Michele, Monica Giannotta, and Alberto Luini. "Coordination of the secretory compartments via inter-organelle signalling." Seminars in Cell & Developmental Biology 20, no. 7 (2009): 801–9. http://dx.doi.org/10.1016/j.semcdb.2009.04.004.

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Canton, Johnathan, and Peter E. Kima. "Interactions of pathogen-containing compartments with the secretory pathway." Cellular Microbiology 14, no. 11 (2012): 1676–86. http://dx.doi.org/10.1111/cmi.12000.

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Carmeille, Romain, Porfirio Schiano Lomoriello, Parvathi M. Devarakonda, Jacob A. Kellermeier, and Aoife T. Heaslip. "Actin and an unconventional myosin motor, TgMyoF, control the organization and dynamics of the endomembrane network in Toxoplasma gondii." PLOS Pathogens 17, no. 2 (2021): e1008787. http://dx.doi.org/10.1371/journal.ppat.1008787.

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Toxoplasma gondii is an obligate intracellular parasite that relies on three distinct secretory organelles, the micronemes, rhoptries, and dense granules, for parasite survival and disease pathogenesis. Secretory proteins destined for these organelles are synthesized in the endoplasmic reticulum (ER) and sequentially trafficked through a highly polarized endomembrane network that consists of the Golgi and multiple post-Golgi compartments. Currently, little is known about how the parasite cytoskeleton controls the positioning of the organelles in this pathway, or how vesicular cargo is traffick

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Anelli, Tiziana, and Paola Panina-Bordignon. "How to Avoid a No-Deal ER Exit." Cells 8, no. 9 (2019): 1051. http://dx.doi.org/10.3390/cells8091051.

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Efficiency and fidelity of protein secretion are achieved thanks to the presence of different steps, located sequentially in time and space along the secretory compartment, controlling protein folding and maturation. After entering into the endoplasmic reticulum (ER), secretory proteins attain their native structure thanks to specific chaperones and enzymes. Only correctly folded molecules are allowed by quality control (QC) mechanisms to leave the ER and proceed to downstream compartments. Proteins that cannot fold properly are instead retained in the ER to be finally destined to proteasomal

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Kuiper, Roland P., and Gerard JM Martens. "Prohormone transport through the secretory pathway of neuroendocrine cells." Biochemistry and Cell Biology 78, no. 3 (2000): 289–98. http://dx.doi.org/10.1139/o00-020.

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En route through the secretory pathway of neuroendocrine cells, prohormones pass a series of membrane-bounded compartments. During this transport, the prohormones are sorted to secretory granules and proteolytically cleaved to bioactive peptides. Recently, progress has been made in a number of aspects concerning secretory protein transport and sorting, particularly with respect to transport events in the early regions of the secretory pathway. In this review we will deal with some of these aspects, including: i) selective exit from the endoplasmic reticulum via COPII-coated vesicles and the po

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Canty-Laird, Elizabeth G., Yinhui Lu, and Karl E. Kadler. "Stepwise proteolytic activation of type I procollagen to collagen within the secretory pathway of tendon fibroblasts in situ." Biochemical Journal 441, no. 2 (2011): 707–17. http://dx.doi.org/10.1042/bj20111379.

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Proteolytic cleavage of procollagen I to collagen I is essential for the formation of collagen fibrils in the extracellular matrix of vertebrate tissues. Procollagen is cleaved by the procollagen N- and C-proteinases, which remove the respective N- and C-propeptides from procollagen. Procollagen processing is initiated within the secretory pathway in tendon fibroblasts, which are adept in assembling an ordered extracellular matrix of collagen fibrils in vivo. It was thought that intracellular processing was restricted to the TGN (trans-Golgi network). In the present study, brefeldin A treatmen

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Campoy, Emanuel Martín, Felipe Carlos Martín Zoppino, and María Isabel Colombo. "The Early Secretory Pathway Contributes to the Growth of theCoxiella-Replicative Niche." Infection and Immunity 79, no. 1 (2010): 402–13. http://dx.doi.org/10.1128/iai.00688-10.

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ABSTRACTCoxiella burnetiiis a Gram-negative obligate intracellular bacterium. After internalization, this bacterium replicates in a large parasitophorous vacuole that has features of both phagolysosomes and autophagosomal compartments. We have previously demonstrated that early after internalizationCoxiellaphagosomes interact with both the endocytic and the autophagic pathways. In this report, we present evidence that theCoxiella-replicative vacuoles (CRVs) also interact with the secretory pathway. Rab1b is a small GTPase responsible for the anterograde transport between the endoplasmic reticu

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Watson, Robert T., Megumi Furukawa, Shian-Huey Chiang, et al. "The Exocytotic Trafficking of TC10 Occurs through both Classical and Nonclassical Secretory Transport Pathways in 3T3L1 Adipocytes." Molecular and Cellular Biology 23, no. 3 (2003): 961–74. http://dx.doi.org/10.1128/mcb.23.3.961-974.2003.

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ABSTRACT To examine the structural determinants necessary for TC10 trafficking, localization, and function in adipocytes, we generated a series of point mutations in the carboxyl-terminal targeting domain of TC10. Wild-type TC10 (TC10/WT) localized to secretory membrane compartments and caveolin-positive lipid raft microdomains at the plasma membrane. Expression of a TC10/C206S point mutant resulted in a trafficking and localization pattern that was indistinguishable from that of TC10/WT. In contrast, although TC10/C209S or the double TC10/C206,209S mutant was plasma membrane localized, it was

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Plutner, H., H. W. Davidson, J. Saraste, and W. E. Balch. "Morphological analysis of protein transport from the ER to Golgi membranes in digitonin-permeabilized cells: role of the P58 containing compartment." Journal of Cell Biology 119, no. 5 (1992): 1097–116. http://dx.doi.org/10.1083/jcb.119.5.1097.

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The glycoside digitonin was used to selectively permeabilize the plasma membrane exposing functionally and morphologically intact ER and Golgi compartments. Permeabilized cells efficiently transported vesicular stomatitis virus glycoprotein (VSV-G) through sealed, membrane-bound compartments in an ATP and cytosol dependent fashion. Transport was vectorial. VSV-G protein was first transported to punctate structures which colocalized with p58 (a putative marker for peripheral punctate pre-Golgi intermediates and the cis-Golgi network) before delivery to the medial Golgi compartments containing a

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Yang, Tao, Hongtao Zeng, Jian Zhang, et al. "MHC class II molecules, cathepsins, and La/SSB proteins in lacrimal acinar cell endomembranes." American Journal of Physiology-Cell Physiology 277, no. 5 (1999): C994—C1007. http://dx.doi.org/10.1152/ajpcell.1999.277.5.c994.

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Sjögren's syndrome is a chronic autoimmune disease affecting the lacrimal glands and other epithelia. It has been suggested that acinar cells of the lacrimal glands provoke local autoimmune responses, leading to Sjögren's syndrome when they begin expressing major histocompatibility complex (MHC) class II molecules. We used isopycnic centrifugation and phase partitioning to resolve compartments that participate in traffic between the basolateral membranes and the endomembrane system to test the hypothesis that MHC class II molecules enter compartments that contain potential autoantigens, i.e.,

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Burkhardt, J. K., S. Hester, C. K. Lapham, and Y. Argon. "The lytic granules of natural killer cells are dual-function organelles combining secretory and pre-lysosomal compartments." Journal of Cell Biology 111, no. 6 (1990): 2327–40. http://dx.doi.org/10.1083/jcb.111.6.2327.

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Cytolytic lymphocytes contain specialized lytic granules whose secretion during cell-mediated cytolysis results in target cell death. Using serial section EM of RNK-16, a natural killer cell line, we show that there are structurally distinct types of granules. Each type is composed of varying proportions of a dense core domain and a multivesicular cortical domain. The dense core domains contain secretory proteins thought to play a role in cytolysis, including cytolysin and chondroitin sulfate proteoglycan. In contrast, the multivesicular domains contain lysosomal proteins, including acid phosp

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Casler, Jason C., Effrosyni Papanikou, Juan J. Barrero, and Benjamin S. Glick. "Maturation-driven transport and AP-1–dependent recycling of a secretory cargo in the Golgi." Journal of Cell Biology 218, no. 5 (2019): 1582–601. http://dx.doi.org/10.1083/jcb.201807195.

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Golgi cisternal maturation has been visualized by fluorescence imaging of individual cisternae in the yeast Saccharomyces cerevisiae, but those experiments did not track passage of a secretory cargo. The expectation is that a secretory cargo will be continuously present within maturing cisternae as resident Golgi proteins arrive and depart. We tested this idea using a regulatable fluorescent secretory cargo that forms ER-localized aggregates, which dissociate into tetramers upon addition of a ligand. The solubilized tetramers rapidly exit the ER and then transit through early and late Golgi co

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