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Journal articles on the topic 'Endomembrane system'

Author: Grafiati

Published: 4 June 2021

Last updated: 18 February 2022

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1

Martínez Jaramillo, Catalina, and Claudia Milena Trujillo Vargas. "LRBA in the endomembrane system." Colombia Médica 49, no. 3 (September 1, 2018): 236–43. http://dx.doi.org/10.25100/cm.v49i3.3802.

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Bi-allelic mutations in LRBA (from Lipopolysaccharide-responsive and beige-like anchor protein) result in a primary immunodeficiency with clinical features ranging from hypogammaglobulinemia and lymphoproliferative syndrome to inflammatory bowel disease and heterogeneous autoimmune manifestations. LRBA deficiency has been shown to affect vesicular trafficking, autophagy and apoptosis, which may lead to alterations of several molecules and processes that play key roles for immunity. In this review, we will discuss the relationship of LRBA with the endovesicular system in the context of receptor trafficking, autophagy and apoptosis. Since these mechanisms of homeostasis are inherent to all living cells and not only limited to the immune system and also, because they are involved in physiological as well as pathological processes such as embryogenesis or tumoral transformation, we envisage advancing in the identification of potential pharmacological agents to manipulate these processes.

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2

Harris, N. "Organization of the Endomembrane System." Annual Review of Plant Physiology 37, no. 1 (June 1986): 73–92. http://dx.doi.org/10.1146/annurev.pp.37.060186.000445.

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3

Soltys, B. J., M. Falah, and R. S. Gupta. "Identification of endoplasmic reticulum in the primitive eukaryote Giardia lamblia using cryoelectron microscopy and antibody to Bip." Journal of Cell Science 109, no. 7 (July 1, 1996): 1909–17. http://dx.doi.org/10.1242/jcs.109.7.1909.

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Giardia lamblia trophozoites contain a complex endomembrane system as demonstrated by fluorescence and cryoelectron microscopy. The endomembrane system was weakly detected in live cells using the fluorescent membrane dye 3,3′-dihexyloxacarbocyanine iodide. The definitive identification of endoplasmic reticulum required the development of a molecular label. We expressed Giardial Bip in Escherichia coli and raised a polyclonal antibody to the purified protein. In western blots, the antibody was specific for Giardial Bip and did not react with human, monkey and rodent homologs. By immunofluorescence microscopy in methanol fixed cells the antibody visualized tubular structures and other subcellular components that required characterization by electron microscopy. Using cryotechniques we directly demonstrate the presence of a complex endomembrane system at the ultrastructural level. In conjunction with Bip immunogold labeling of cryosections we identify: (1) endoplasmic reticulum cisternae and tubules; (2) stacked perinuclear membranes; and (3) Bip presence in the nuclear envelope. Both the endoplasmic reticulum and nuclear envelope were found either with or without a cleft region suggesting each may contain common specialized sub-regions. In stacked perinuclear membranes, which may represent either multilamellar endoplasmic reticulum or a Golgi apparatus, Bip labeling was restricted to peripheral layers, also suggesting specialized sub-regions. Labeled endomembrane systems could be observed associated with microtubule structures, including axonemes and the adhesive disk. The presence of an extensive endomembrane system in Giardia lamblia, which represents one of the earliest diverging eukaryotic species, supports the view that both the nucleus and endomembrane system co-evolved in a common ancestor of eukaryotic cells.

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4

Shen, Jinbo, Yonglun Zeng, Xiaohong Zhuang, Lei Sun, Xiaoqiang Yao, Peter Pimpl, and Liwen Jiang. "Organelle pH in the Arabidopsis Endomembrane System." Molecular Plant 6, no. 5 (September 2013): 1419–37. http://dx.doi.org/10.1093/mp/sst079.

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5

Kumar, A., and B. McClure. "Pollen-pistil interactions and the endomembrane system." Journal of Experimental Botany 61, no. 7 (April 1, 2010): 2001–13. http://dx.doi.org/10.1093/jxb/erq065.

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6

Day, Kasey J., Jason C. Casler, and Benjamin S. Glick. "Budding Yeast Has a Minimal Endomembrane System." Developmental Cell 44, no. 1 (January 2018): 56–72. http://dx.doi.org/10.1016/j.devcel.2017.12.014.

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7

Grissom, James H., Verónica A. Segarra, and Richard J. Chi. "New Perspectives on SNARE Function in the Yeast Minimal Endomembrane System." Genes 11, no. 8 (August 6, 2020): 899. http://dx.doi.org/10.3390/genes11080899.

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Saccharomyces cerevisiae is one of the best model organisms for the study of endocytic membrane trafficking. While studies in mammalian cells have characterized the temporal and morphological features of the endocytic pathway, studies in budding yeast have led the way in the analysis of the endosomal trafficking machinery components and their functions. Eukaryotic endomembrane systems were thought to be highly conserved from yeast to mammals, with the fusion of plasma membrane-derived vesicles to the early or recycling endosome being a common feature. Upon endosome maturation, cargos are then sorted for reuse or degraded via the endo-lysosomal (endo-vacuolar in yeast) pathway. However, recent studies have shown that budding yeast has a minimal endomembrane system that is fundamentally different from that of mammalian cells, with plasma membrane-derived vesicles fusing directly to a trans-Golgi compartment which acts as an early endosome. Thus, the Golgi, rather than the endosome, acts as the primary acceptor of endocytic vesicles, sorting cargo to pre-vacuolar endosomes for degradation. The field must now integrate these new findings into a broader understanding of the endomembrane system across eukaryotes. This article synthesizes what we know about the machinery mediating endocytic membrane fusion with this new model for yeast endomembrane function.

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8

Titorenko, Vladimir I., and Robert T. Mullen. "Peroxisome biogenesis: the peroxisomal endomembrane system and the role of the ER." Journal of Cell Biology 174, no. 1 (June 26, 2006): 11–17. http://dx.doi.org/10.1083/jcb.200604036.

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Peroxisomes have long been viewed as semiautonomous, static, and homogenous organelles that exist outside the secretory and endocytic pathways of vesicular flow. However, growing evidence supports the view that peroxisomes actually constitute a dynamic endomembrane system that originates from the endoplasmic reticulum. This review highlights the various strategies used by evolutionarily diverse organisms for coordinating the flow of membrane-enclosed carriers through the peroxisomal endomembrane system and critically evaluates the dynamics and molecular mechanisms of this multistep process.

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9

Tsyrkunov, V. M., V. P. Andreev, and R. I. Kravchuk. "CLINICAL MORPHOLOGY OF THE LIVER: HEPATOCYTES, ENDOMEMBRANE SYSTEM." Hepatology and Gastroenterology 3, no. 1 (2019): 28–42. http://dx.doi.org/10.25298/2616-5546-2019-3-1-28-42.

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10

Martone, Maryann E., Victoria M. Simpliciano, Ying Zhang, Thomas J. Deerinck, and Mark H. Ellisman. "Structure and function of the neuronal endomembrane system." Proceedings, annual meeting, Electron Microscopy Society of America 51 (August 1, 1993): 98–99. http://dx.doi.org/10.1017/s0424820100146333.

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Components of the endomembrane system in a variety of cell types appear to function in the storage and release of calcium similar to the muscle sarcoplasmic reticulum. Many proteins involved in intracellular calcium regulation in skeletal or smooth muscle, e.g. Ca++ ATPase, calsequestrin, the inositol l,4,5,trisphosphate (TP3) receptor and the ryanodine binding protein, are found in the nervous system where they are particularly abundant within the smooth endoplasmic reticulum (SER) of cerebellar Purkinje neurons. Immunolocalization studies suggest, however, that calcium regulatory proteins are not uniformly distributed within the SER but are concentrated in or excluded from certain domains. For example, the IP3 and ryanodine receptors, two distinct calcium channels which mediate calcium release by different ligands, are found associated with the SER in cell bodies and dendrites of chick cerebellum but only the IP3 receptor is found within dendritic spines. These results are consistent with evidence that cells may possess multiple intracellular calcium stores that are pharmacologically, spatially and perhaps physically distinct.

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11

Dacks, Joel B., Andrew A. Peden, and Mark C. Field. "Evolution of specificity in the eukaryotic endomembrane system." International Journal of Biochemistry & Cell Biology 41, no. 2 (February 2009): 330–40. http://dx.doi.org/10.1016/j.biocel.2008.08.041.

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12

Farhan, Hesso, Mondira Kundu, and Susan Ferro-Novick. "The link between autophagy and secretion: a story of multitasking proteins." Molecular Biology of the Cell 28, no. 9 (May 2017): 1161–64. http://dx.doi.org/10.1091/mbc.e16-11-0762.

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The secretory and autophagy pathways can be thought of as the biosynthetic (i.e., anabolic) and degradative (i.e., catabolic) branches of the endomembrane system. In analogy to anabolic and catabolic pathways in metabolism, there is mounting evidence that the secretory and autophagy pathways are intimately linked and that certain regulatory elements are shared between them. Here we highlight the parallels and points of intersection between these two evolutionarily highly conserved and fundamental endomembrane systems. The intersection of these pathways may play an important role in remodeling membranes during cellular stress.

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13

Gal, Susannah, and Natasha V. Raikhel. "Protein sorting in the endomembrane system of plant cells." Current Opinion in Cell Biology 5, no. 4 (August 1993): 636–40. http://dx.doi.org/10.1016/0955-0674(93)90133-b.

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14

Rawe, V. Y., A. J. Español, F. Nodar, and S. Brugo Olmedo. "Mammalian Oocyte in Vitro Maturation: The Endomembrane System Dynamics." Fertility and Sterility 84 (September 2005): S420. http://dx.doi.org/10.1016/j.fertnstert.2005.07.1098.

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15

Ozansoy, Mehmet, and Yagmur Denizhan. "The Endomembrane System: A Representation of the Extracellular Medium?" Biosemiotics 2, no. 3 (October 13, 2009): 255–67. http://dx.doi.org/10.1007/s12304-009-9063-3.

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16

Markgraf, Daniel F., Karolina Peplowska, and Christian Ungermann. "Rab cascades and tethering factors in the endomembrane system." FEBS Letters 581, no. 11 (February 12, 2007): 2125–30. http://dx.doi.org/10.1016/j.febslet.2007.01.090.

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17

Okita, Thomas W., and John C. Rogers. "COMPARTMENTATION OF PROTEINS IN THE ENDOMEMBRANE SYSTEM OF PLANT CELLS." Annual Review of Plant Physiology and Plant Molecular Biology 47, no. 1 (June 1996): 327–50. http://dx.doi.org/10.1146/annurev.arplant.47.1.327.

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18

Matsuoka, Ken, and Sebastian Y. Bednarek. "Protein transport within the plant cell endomembrane system: an update." Current Opinion in Plant Biology 1, no. 6 (December 1998): 463–69. http://dx.doi.org/10.1016/s1369-5266(98)80036-8.

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19

Satiat-Jeunemaître, Béatrice, Fabien Gaire, and Spencer Brown. "Dynamics of the endomembrane system in plant cells: Immunocytochemical studies." Biology of the Cell 90, no. 3 (June 1998): 265–66. http://dx.doi.org/10.1016/s0248-4900(98)80031-2.

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20

Ostrowicz, Clemens W., Christoph T. A. Meiringer, and Christian Ungermann. "Yeast vacuole fusion: A model system for eukaryotic endomembrane dynamics." Autophagy 4, no. 1 (January 2008): 5–19. http://dx.doi.org/10.4161/auto.5054.

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21

Mari, Muriel, and Fulvio Reggiori. "Atg9 reservoirs, a new organelle of the yeast endomembrane system?" Autophagy 6, no. 8 (November 16, 2010): 1221–23. http://dx.doi.org/10.4161/auto.6.8.13792.

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22

Vitale, A. "Recombinant Pharmaceuticals from Plants: The Plant Endomembrane System as Bioreactor." Molecular Interventions 5, no. 4 (August 1, 2005): 216–25. http://dx.doi.org/10.1124/mi.5.4.5.

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23

Santarella-Mellwig, Rachel, Sabine Pruggnaller, Norbert Roos, Iain W. Mattaj, and Damien P. Devos. "Three-Dimensional Reconstruction of Bacteria with a Complex Endomembrane System." PLoS Biology 11, no. 5 (May 21, 2013): e1001565. http://dx.doi.org/10.1371/journal.pbio.1001565.

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24

Nürnberg, Bernd, and Gudrun Ahnert-Hilger. "Potential roles of heterotrimeric G proteins of the endomembrane system." FEBS Letters 389, no. 1 (June 24, 1996): 61–65. http://dx.doi.org/10.1016/0014-5793(96)00584-4.

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25

Dunkley, T. P. J., P. Dupree, R. B. Watson, and K. S. Lilley. "The use of isotope-coded affinity tags (ICAT) to study organelle proteomes in Arabidopsis thaliana." Biochemical Society Transactions 32, no. 3 (June 1, 2004): 520–23. http://dx.doi.org/10.1042/bst0320520.

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Organelle proteomics is the analysis of the protein contents of a subcellular compartment. Proteins identified in subcellular proteomic studies can only be assigned to an organelle if there are no contaminants present in the sample preparation. As a result, the majority of plant organelle proteomic studies have focused on the chloroplast and mitochondria, which can be isolated relatively easily. However, the isolation of components of the endomembrane system is far more difficult due to their similar sizes and densities. For this reason, quantitative proteomics methods are being developed to enable the assignment of proteins to a specific component of the endomembrane system without the need to obtain pure organelles.

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26

Domozych, David S., Li Sun, Kattia Palacio-Lopez, Reagan Reed, Susan Jeon, Mingjia Li, Chen Jiao, Iben Sørensen, Zhangjun Fei, and Jocelyn K. C. Rose. "Endomembrane architecture and dynamics during secretion of the extracellular matrix of the unicellular charophyte, Penium margaritaceum." Journal of Experimental Botany 71, no. 11 (February 25, 2020): 3323–39. http://dx.doi.org/10.1093/jxb/eraa039.

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Abstract The extracellular matrix (ECM) of many charophytes, the assemblage of green algae that are the sister group to land plants, is complex, produced in large amounts, and has multiple essential functions. An extensive secretory apparatus and endomembrane system are presumably needed to synthesize and secrete the ECM, but structural details of such a system have not been fully characterized. Penium margaritaceum is a valuable unicellular model charophyte for studying secretion dynamics. We report that Penium has a highly organized endomembrane system, consisting of 150–200 non-mobile Golgi bodies that process and package ECM components into different sets of vesicles that traffic to the cortical cytoplasm, where they are transported around the cell by cytoplasmic streaming. At either fixed or transient areas, specific cytoplasmic vesicles fuse with the plasma membrane and secrete their constituents. Extracellular polysaccharide (EPS) production was observed to occur in one location of the Golgi body and sometimes in unique Golgi hybrids. Treatment of cells with brefeldin A caused disruption of the Golgi body, and inhibition of EPS secretion and cell wall expansion. The structure of the endomembrane system in Penium provides mechanistic insights into how extant charophytes generate large quantities of ECM, which in their ancestors facilitated the colonization of land.

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27

Dell'Angelica, Esteban C., and Juan S. Bonifacino. "Coatopathies: Genetic Disorders of Protein Coats." Annual Review of Cell and Developmental Biology 35, no. 1 (October 6, 2019): 131–68. http://dx.doi.org/10.1146/annurev-cellbio-100818-125234.

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Protein coats are supramolecular complexes that assemble on the cytosolic face of membranes to promote cargo sorting and transport carrier formation in the endomembrane system of eukaryotic cells. Several types of protein coats have been described, including COPI, COPII, AP-1, AP-2, AP-3, AP-4, AP-5, and retromer, which operate at different stages of the endomembrane system. Defects in these coats impair specific transport pathways, compromising the function and viability of the cells. In humans, mutations in subunits of these coats cause various congenital diseases that are collectively referred to as coatopathies. In this article, we review the fundamental properties of protein coats and the diseases that result from mutation of their constituent subunits.

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28

Ruano, Guillermo, and David Scheuring. "Plant Cells under Attack: Unconventional Endomembrane Trafficking during Plant Defense." Plants 9, no. 3 (March 21, 2020): 389. http://dx.doi.org/10.3390/plants9030389.

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Since plants lack specialized immune cells, each cell has to defend itself independently against a plethora of different pathogens. Therefore, successful plant defense strongly relies on precise and efficient regulation of intracellular processes in every single cell. Smooth trafficking within the plant endomembrane is a prerequisite for a diverse set of immune responses. Pathogen recognition, signaling into the nucleus, cell wall enforcement, secretion of antimicrobial proteins and compounds, as well as generation of reactive oxygen species, all heavily depend on vesicle transport. In contrast, pathogens have developed a variety of different means to manipulate vesicle trafficking to prevent detection or to inhibit specific plant responses. Intriguingly, the plant endomembrane system exhibits remarkable plasticity upon pathogen attack. Unconventional trafficking pathways such as the formation of endoplasmic reticulum (ER) bodies or fusion of the vacuole with the plasma membrane are initiated and enforced as the counteraction. Here, we review the recent findings on unconventional and defense-induced trafficking pathways as the plant´s measures in response to pathogen attack. In addition, we describe the endomembrane system manipulations by different pathogens, with a focus on tethering and fusion events during vesicle trafficking.

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29

Satiat-Jeunemaitre, Béatrice, Jancy Henderson, David Evans, Kim Crooks, Mark Fricker, Richard Napier, and Chris Hawes. "Brefeldin A affects the endomembrane system and vesicle trafficking in higher plants." Proceedings, annual meeting, Electron Microscopy Society of America 51 (August 1, 1993): 192–93. http://dx.doi.org/10.1017/s0424820100146801.

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In plant cells, as in animal cells, many macromolecules and membranes are transported by vesicle vectors through both the exocytotic and endocytotic pathways. In order to elucidate the mechanisms and molecular events of such trafficking we are using a set of drugs known to perturb membrane flow in plant cells in combination with immunocytochemical studies using a bank of monoclonal antibodies to various components of the endomembrane system and cell surface. In animal cells, one such drug, Brefeldin A, a fungal fatty acid derivative which causes disruption of the Golgi apparatus, has recently been used as a tool to dissect the mechanisms of vesicle flow from the endoplasmic reticulum to the Golgi apparatus and down the cisternae of the Golgi stack (1). It has been demonstrated that BFA also has a dramatic effect on the Golgi apparatus in higher plant cells (2,3,4).In this paper we report on recent work on the disruption of the plant Golgi apparatus with BFA and the redistribution of endomembrane marker epitopes after drug treatment of roots and suspension culture cells.

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30

Fiske, Michael, Michael White, Stephanie Valtierra, Sara Herrera, Keith Solvang, Alina Konnikova, and Shubhik DebBurman. "Familial Parkinson's Disease Mutant E46K α-Synuclein Localizes to Membranous Structures, Forms Aggregates, and Induces Toxicity in Yeast Models." ISRN Neurology 2011 (July 9, 2011): 1–14. http://dx.doi.org/10.5402/2011/521847.

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In Parkinson’s disease (PD), midbrain dopaminergic neuronal death is linked to the accumulation of aggregated α-synuclein. The familial PD mutant form of α-synuclein, E46K, has not been thoroughly evaluated yet in an organismal model system. Here, we report that E46K resembled wild-type (WT) α-synuclein in Saccharomyces cerevisiae in that it predominantly localized to the plasma membrane, and it did not induce significant toxicity or accumulation. In contrast, in Schizosaccharomyces pombe, E46K did not associate with the plasma membrane. Instead, in one strain, it extensively aggregated in the cytoplasm and was as toxic as WT. Remarkably, in another strain, E46K extensively associated with the endomembrane system and was more toxic than WT. Our studies recapitulate and extend aggregation and phospholipid membrane association properties of E46K previously observed in vitro and cell culture. Furthermore, it supports the notion that E46K generates toxicity partly due to increased association with endomembrane systems within cells.

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31

Wiser, Mark F. "Unique Endomembrane Systems and Virulence in Pathogenic Protozoa." Life 11, no. 8 (August 12, 2021): 822. http://dx.doi.org/10.3390/life11080822.

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Virulence in pathogenic protozoa is often tied to secretory processes such as the expression of adhesins on parasite surfaces or the secretion of proteases to assisted in tissue invasion and other proteins to avoid the immune system. This review is a broad overview of the endomembrane systems of pathogenic protozoa with a focus on Giardia, Trichomonas, Entamoeba, kinetoplastids, and apicomplexans. The focus is on unique features of these protozoa and how these features relate to virulence. In general, the basic elements of the endocytic and exocytic pathways are present in all protozoa. Some of these elements, especially the endosomal compartments, have been repurposed by the various species and quite often the repurposing is associated with virulence. The Apicomplexa exhibit the most unique endomembrane systems. This includes unique secretory organelles that play a central role in interactions between parasite and host and are involved in the invasion of host cells. Furthermore, as intracellular parasites, the apicomplexans extensively modify their host cells through the secretion of proteins and other material into the host cell. This includes a unique targeting motif for proteins destined for the host cell. Most notable among the apicomplexans is the malaria parasite, which extensively modifies and exports numerous proteins into the host erythrocyte. These modifications of the host erythrocyte include the formation of unique membranes and structures in the host erythrocyte cytoplasm and on the erythrocyte membrane. The transport of parasite proteins to the host erythrocyte involves several unique mechanisms and components, as well as the generation of compartments within the erythrocyte that participate in extraparasite trafficking.

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32

Barlow, S. B., and R. E. Triemer. "Phosphatase localization in the endomembrane system of the dinoflagellate Crypthecodinium cohnii." Journal of Histochemistry & Cytochemistry 34, no. 8 (August 1986): 1021–27. http://dx.doi.org/10.1177/34.8.3016072.

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The distribution of four enzymes within the endomembrane system of the protist Crypthecodinium cohnii has been determined using cytochemical localizations with lead as a capture agent. Nucleoside diphosphatase (NDPase) activity, using inosine diphosphate (IDP) and thiamine pyrophosphate (TPP) as substrates, was observed in the Golgi apparatus, with a gradient of increasing reaction product noted in some cells from the cis to trans cisternae. Tubules and vesicles associated with the trans cisternae also contained reaction product. The endoplasmic reticulum exhibited a high activity of glucose-6-phosphatase [with glucose-6-phosphate (G-6-P) as substrate]. Traces of reaction product were also observed in the cis-most and trans-most cisternae of the dictyosomes. Activity of acid phosphatase (AcPase) was observed in Golgi cisternae as well as in associated cytoplasmic vesicles. Heaviest deposition was localized in medial and trans dictyosome cisternae. The cytoplasmic system of flattened vesicles subtending the surface membranes in these cells did not exhibit reactivity with any of the substrates used. The distribution of these enzymes in this algal cell appears similar to that observed in animal cells and suggests that these enzymes may represent markers for algal cell endomembrane compartments.

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González-Sánchez, Juan, Ricardo Costa, and Damien Devos. "A Multi-Functional Tubulovesicular Network as the Ancestral Eukaryotic Endomembrane System." Biology 4, no. 2 (March 24, 2015): 264–81. http://dx.doi.org/10.3390/biology4020264.

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34

Schumacher, Karin. "pH in the plant endomembrane system — an import and export business." Current Opinion in Plant Biology 22 (December 2014): 71–76. http://dx.doi.org/10.1016/j.pbi.2014.09.005.

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35

Moore, Ian, and Angus Murphy. "Validating the Location of Fluorescent Protein Fusions in the Endomembrane System." Plant Cell 21, no. 6 (June 2009): 1632–36. http://dx.doi.org/10.1105/tpc.109.068668.

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36

Simpson, Jeremy C. "Modification of the Mammalian Endomembrane System in Healthy and Diseased Cells." International Journal of Molecular Sciences 21, no. 6 (March 20, 2020): 2133. http://dx.doi.org/10.3390/ijms21062133.

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37

Lippincott-Schwartz, Jennifer, and Robert D. Phair. "Lipids and Cholesterol as Regulators of Traffic in the Endomembrane System." Annual Review of Biophysics 39, no. 1 (April 2010): 559–78. http://dx.doi.org/10.1146/annurev.biophys.093008.131357.

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38

Vitale, Alessandro, and Gad Galili. "The Endomembrane System and the Problem of Protein Sorting: Fig. 1." Plant Physiology 125, no. 1 (January 1, 2001): 115–18. http://dx.doi.org/10.1104/pp.125.1.115.

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39

Elias, Marek. "Patterns and processes in the evolution of the eukaryotic endomembrane system." Molecular Membrane Biology 27, no. 8 (November 2010): 469–89. http://dx.doi.org/10.3109/09687688.2010.521201.

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40

Minamino, Naoki, Takehiko Kanazawa, Ryuichi Nishihama, Katsuyuki T. Yamato, Kimitsune Ishizaki, Takayuki Kohchi, Akihiko Nakano, and Takashi Ueda. "Dynamic reorganization of the endomembrane system during spermatogenesis in Marchantia polymorpha." Journal of Plant Research 130, no. 3 (February 3, 2017): 433–41. http://dx.doi.org/10.1007/s10265-017-0909-5.

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41

Brighouse, Andrew, Joel B. Dacks, and Mark C. Field. "Rab protein evolution and the history of the eukaryotic endomembrane system." Cellular and Molecular Life Sciences 67, no. 20 (June 26, 2010): 3449–65. http://dx.doi.org/10.1007/s00018-010-0436-1.

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42

Zingen-Sell, Irmgard, S. Hillmer, D. G. Robinson, and R. L. Jones. "Localization of ?-amylase isozymes within the endomembrane system of barley aleurone." Protoplasma 154, no. 1 (February 1990): 16–24. http://dx.doi.org/10.1007/bf01349531.

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43

Qian, Limin, Tao Yang, Haishan Chen, Jiansong Xie, Hongtao Zeng, Dwight W. Warren, Michaela MacVeigh, Michele A. Meneray, Sarah F. Hamm-Alvarez, and Austin K. Mircheff. "Heterotrimeric GTP-binding Proteins in the Lacrimal Acinar Cell Endomembrane System." Experimental Eye Research 74, no. 1 (January 2002): 7–22. http://dx.doi.org/10.1006/exer.2001.1108.

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44

Crofts, Andrew J., Haruhiko Washida, Thomas W. Okita, Mio Satoh, Masahiro Ogawa, Toshihiro Kumamaru, and Hikaru Satoh. "The role of mRNA and protein sorting in seed storage protein synthesis, transport, and deposition." Biochemistry and Cell Biology 83, no. 6 (December 1, 2005): 728–37. http://dx.doi.org/10.1139/o05-156.

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Rice synthesizes and accumulates high levels of 2 distinct classes of seed storage proteins and sorts them to separate intracellular compartments, making it an ideal model system for studying the mechanisms of storage protein synthesis, transport, and deposition. In rice, RNA localization dictates the initial site of storage protein synthesis on specific subdomains of the cortical endoplasmic reticulum (ER), and there is a direct relation between the RNA localization site and the final destination of the encoded protein within the endomembrane system. Current data support the existence of 3 parallel RNA localization pathways leading from the nucleus to the actively synthesizing cortical ER. Additional pathways may exist for the synthesis of cytoplasmic and nuclear-encoded proteins targeted to organelles, the latter located in a stratified arrangement in developing endosperm cells. The study of rice mutants, which accumulate unprocessed glutelin precursors, indicates that these multiple pathways prevent nonproductive interactions between different classes of storage proteins that would otherwise disrupt protein sorting. Indeed, it appears that the prevention of disruptive interactions between different classes of storage proteins plays a key role in their biosynthesis in rice. In addition to highlighting the unique features of the plant endomembrane system and describing the relation between RNA and protein localization, this minireview will attempt to address a number of questions raised by recent studies on these processes.Key words: mRNA localization, protein localization, endomembrane system, seed storage proteins, rice.

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Morita, Miyo Terao, and Tomoo Shimada. "The Plant Endomembrane System—A Complex Network Supporting Plant Development and Physiology." Plant and Cell Physiology 55, no. 4 (April 2014): 667–71. http://dx.doi.org/10.1093/pcp/pcu049.

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Gould, Sven B., Sriram G. Garg, and William F. Martin. "Bacterial Vesicle Secretion and the Evolutionary Origin of the Eukaryotic Endomembrane System." Trends in Microbiology 24, no. 7 (July 2016): 525–34. http://dx.doi.org/10.1016/j.tim.2016.03.005.

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Brandizzi, F., S. L. Irons, J. Johansen, A. Kotzer, and U. Neumann. "GFP is the way to glow: bioimaging of the plant endomembrane system." Journal of Microscopy 214, no. 2 (May 2004): 138–58. http://dx.doi.org/10.1111/j.0022-2720.2004.01334.x.

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Sparkes, Imogen, and Federica Brandizzi. "Fluorescent protein-based technologies: shedding new light on the plant endomembrane system." Plant Journal 70, no. 1 (March 27, 2012): 96–107. http://dx.doi.org/10.1111/j.1365-313x.2011.04884.x.

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Helm, K. W., P. R. LaFayette, R. T. Nagao, J. L. Key, and E. Vierling. "Localization of small heat shock proteins to the higher plant endomembrane system." Molecular and Cellular Biology 13, no. 1 (January 1993): 238–47. http://dx.doi.org/10.1128/mcb.13.1.238.

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Three related gene families of low-molecular-weight (LMW) heat shock proteins (HSPs) have been characterized in plants. We describe a fourth LMW HSP family, represented by PsHSP22.7 from Pisum sativum and GmHSP22.0 from Glycine max, and demonstrate that this family of proteins is endomembrane localized. PsHSP22.7 and GmHSP22.0 are 76.7% identical at the amino acid level. Both proteins have amino-terminal signal peptides and carboxyl-terminal sequences characteristic of endoplasmic reticulum (ER) retention signals. The two proteins closely resemble class I cytoplasmic LMW HSPs, suggesting that they evolved from the cytoplasmic proteins through the addition of the signal peptide and ER retention motif. The endomembrane localization of these proteins was confirmed by cell fractionation. The polypeptide product of PsHSP22.7 mRNA was processed to a smaller-M(r) form by canine pancreatic microsomes; in vivo, GmHSP22.0 polysomal mRNA was found to be predominantly membrane bound. In vitro-processed PsHSP22.7 corresponded in mass and pI to one of two proteins detected in ER fractions from heat-stressed plants by using anti-PsHSP22.7 antibodies. Like other LMW HSPs, PsHSP22.7 was observed in higher-molecular-weight structures with apparent masses of between 80 and 240 kDa. The results reported here indicate that members of this new class of LMW HSPs are most likely resident ER proteins and may be similar in function to related LMW HSPs in the cytoplasm. Along with the HSP90 and HSP70 classes of HSPs, this is the third category of HSPs localized to the ER.

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Nagy, Peter D., and Zhike Feng. "Tombusviruses orchestrate the host endomembrane system to create elaborate membranous replication organelles." Current Opinion in Virology 48 (June 2021): 30–41. http://dx.doi.org/10.1016/j.coviro.2021.03.007.

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