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Thematische Bibliographien / Vesicular transport proteins / Zeitschriftenartikel

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Zeitschriftenartikel zum Thema „Vesicular transport proteins“

Autor: Grafiati

Veröffentlicht am 4. Juni 2021

Zuletzt aktualisiert am 13. Februar 2022

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1

NAKANO, AKIHIKO. "Vesicular Transport of Proteins in Yeast." RADIOISOTOPES 44, no. 3 (1995): 221–22. http://dx.doi.org/10.3769/radioisotopes.44.221.

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Balch, William E. "Small GTP-binding proteins in vesicular transport." Trends in Biochemical Sciences 15, no. 12 (1990): 473–77. http://dx.doi.org/10.1016/0968-0004(90)90301-q.

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Kurzchalia, T. V., P. Dupree, R. G. Parton, et al. "VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles." Journal of Cell Biology 118, no. 5 (1992): 1003–14. http://dx.doi.org/10.1083/jcb.118.5.1003.

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In simple epithelial cells, apical and basolateral proteins are sorted into separate vesicular carriers before delivery to the appropriate plasma membrane domains. To dissect the putative sorting machinery, we have solubilized Golgi-derived transport vesicles with the detergent CHAPS and shown that an apical marker, influenza haemagglutinin (HA), formed a large complex together with several integral membrane proteins. Remarkably, a similar set of CHAPS-insoluble proteins was found after solubilization of a total cellular membrane fraction. This allowed the cloning of a cDNA encoding one protei

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Stow, Jennifer L. "Regulation of vesicular transport by GTP-binding proteins." Current Opinion in Nephrology and Hypertension 4, no. 5 (1995): 421–25. http://dx.doi.org/10.1097/00041552-199509000-00009.

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Waters, M. Gerard, Irene C. Griff, and James E. Rothman. "Proteins involved in vesicular transport and membrane fusion." Current Opinion in Cell Biology 3, no. 4 (1991): 615–20. http://dx.doi.org/10.1016/0955-0674(91)90031-s.

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6

Advani, Raj J., Bin Yang, Rytis Prekeris, Kelly C. Lee, Judith Klumperman, and Richard H. Scheller. "Vamp-7 Mediates Vesicular Transport from Endosomes to Lysosomes." Journal of Cell Biology 146, no. 4 (1999): 765–76. http://dx.doi.org/10.1083/jcb.146.4.765.

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A more complete picture of the molecules that are critical for the organization of membrane compartments is beginning to emerge through the characterization of proteins in the vesicle-associated membrane protein (also called synaptobrevin) family of membrane trafficking proteins. To better understand the mechanisms of membrane trafficking within the endocytic pathway, we generated a series of monoclonal and polyclonal antibodies against the cytoplasmic domain of vesicle-associated membrane protein 7 (VAMP-7). The antibodies recognize a 25-kD membrane-associated protein in multiple tissues and

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Martínez-Menárguez, José A., Rytis Prekeris, Viola M. J. Oorschot, et al. "Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport." Journal of Cell Biology 155, no. 7 (2001): 1213–24. http://dx.doi.org/10.1083/jcb.200108029.

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A cisternal progression mode of intra-Golgi transport requires that Golgi resident proteins recycle by peri-Golgi vesicles, whereas the alternative model of vesicular transport predicts anterograde cargo proteins to be present in such vesicles. We have used quantitative immuno-EM on NRK cells to distinguish peri-Golgi vesicles from other vesicles in the Golgi region. We found significant levels of the Golgi resident enzyme mannosidase II and the transport machinery proteins giantin, KDEL-receptor, and rBet1 in coatomer protein I–coated cisternal rims and peri-Golgi vesicles. By contrast, when

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Predescu, Dan, Stephen M. Vogel, and Asrar B. Malik. "Functional and morphological studies of protein transcytosis in continuous endothelia." American Journal of Physiology-Lung Cellular and Molecular Physiology 287, no. 5 (2004): L895—L901. http://dx.doi.org/10.1152/ajplung.00075.2004.

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Continuous microvascular endothelium constitutively transfers protein from vessel lumen to interstitial space. Compelling recent biochemical, ultrastructural, and physiological evidence reviewed herein demonstrates that protein transport is not the result of barrier “leakiness” but, rather, is an active process occurring primarily in a transendothelial vesicular pathway. Protein accesses the vesicular pathway by means of caveolae open to the vessel lumen. Vascular tracer proteins appear in free cytoplasmic vesicles within minutes; contents of transport vesicles are rapidly deposited into the s

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Chaudhari, Rahul, Vishakha Dey, Aishwarya Narayan, Shobhona Sharma, and Swati Patankar. "Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasitePlasmodium falciparum." PeerJ 5 (April 27, 2017): e3128. http://dx.doi.org/10.7717/peerj.3128.

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The secretory pathway inPlasmodium falciparumhas evolved to transport proteins to the host cell membrane and to an endosymbiotic organelle, the apicoplast. The latter can occur via the ER or the ER-Golgi route. Here, we study these three routes using proteins Erythrocyte Membrane Protein-1 (PfEMP1), Acyl Carrier Protein (ACP) and glutathione peroxidase-like thioredoxin peroxidase (PfTPxGl) and inhibitors of vesicular transport. As expected, the G protein-dependent vesicular fusion inhibitor AlF4−and microtubule destabilizing drug vinblastine block the trafficking of PfEMP-1, a protein secreted

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FAIRN, Gregory D., and Christopher R. McMASTER. "Identification and assessment of the role of a nominal phospholipid binding region of ORP1S (oxysterol-binding-protein-related protein 1 short) in the regulation of vesicular transport." Biochemical Journal 387, no. 3 (2005): 889–96. http://dx.doi.org/10.1042/bj20041915.

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The ORPs (oxysterol-binding-protein-related proteins) constitute an enigmatic family of intracellular lipid receptors that are related through a shared lipid binding domain. Emerging evidence suggests that ORPs relate lipid metabolism to membrane transport. Current data imply that the yeast ORP Kes1p is a negative regulator of Golgi-derived vesicular transport mediated by the essential phosphatidylinositol/phosphatidylcholine transfer protein Sec14p. Inactivation of Kes1p function allows restoration of growth and vesicular transport in cells lacking Sec14p function, and Kes1p function in this

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Davidson, H. W., C. H. McGowan, and W. E. Balch. "Evidence for the regulation of exocytic transport by protein phosphorylation." Journal of Cell Biology 116, no. 6 (1992): 1343–55. http://dx.doi.org/10.1083/jcb.116.6.1343.

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We investigated the effects of the protein phosphatase inhibitors okadaic acid and microcystin-LR upon transport of newly synthesized proteins through the exocytic pathway. Treatment of CHO cells with 1 microM okadaic acid rapidly inhibited movement of a marker protein (vesicular stomatitis virus G protein) from the endoplasmic reticulum to the Golgi compartment. Both okadaic acid and microcystin-LR also inhibited transport in an in vitro assay reconstituting movement to the Golgi compartment, at concentrations equivalent to those required to inhibit phosphorylase phosphatase activity. Inhibit

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Goody, Roger Sidney, Matthias Philipp Müller, and Yao-Wen Wu. "Mechanisms of action of Rab proteins, key regulators of intracellular vesicular transport." Biological Chemistry 398, no. 5-6 (2017): 565–75. http://dx.doi.org/10.1515/hsz-2016-0274.

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Abstract Our understanding of the manner in which Rab proteins regulate intracellular vesicular transport has progressed remarkably in the last one or two decades by application of a wide spectrum of biochemical, biophysical and cell biological methods, augmented by the methods of chemical biology. Important additional insights have arisen from examination of the manner in which certain bacteria can manipulate vesicular transport mechanisms. The progress in these areas is summarized here.

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Matsuzaki, Fumiko, Michiko Shirane, Masaki Matsumoto, and Keiichi I. Nakayama. "Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation." Molecular Biology of the Cell 22, no. 23 (2011): 4602–20. http://dx.doi.org/10.1091/mbc.e11-01-0068.

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Neurons are highly polarized cells with long neurites. Vesicular transport is required for neurite extension. We recently identified protrudin as a key regulator of vesicular transport during neurite extension. Expression of protrudin in nonneuronal cells thus induces formation of neurite-like membrane protrusions. We adopted a proteomics approach to identify proteins that associate with protrudin. Among the protrudin-associated proteins, including many with a function related to intracellular trafficking, we focused on KIF5, a motor protein that mediates anterograde vesicular transport in neu

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Béthune, Julien, and Felix T. Wieland. "Assembly of COPI and COPII Vesicular Coat Proteins on Membranes." Annual Review of Biophysics 47, no. 1 (2018): 63–83. http://dx.doi.org/10.1146/annurev-biophys-070317-033259.

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In eukaryotes, distinct transport vesicles functionally connect various intracellular compartments. These carriers mediate transport of membranes for the biogenesis and maintenance of organelles, secretion of cargo proteins and peptides, and uptake of cargo into the cell. Transport vesicles have distinct protein coats that assemble on a donor membrane where they can select cargo and curve the membrane to form a bud. A multitude of structural elements of coat proteins have been solved by X-ray crystallography. More recently, the architectures of the COPI and COPII coats were elucidated in conte

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Cheung, Cecilia Y., Debra F. Anderson, and Robert A. Brace. "Multiomics analyses of vesicular transport pathway-specific transcripts and proteins in ovine amnion: responses to altered intramembranous transport." Physiological Genomics 51, no. 7 (2019): 267–78. http://dx.doi.org/10.1152/physiolgenomics.00003.2019.

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Amniotic fluid volume (AFV) is determined by the rate of intramembranous (IM) transport of amniotic fluid (AF) across the amnion. This transport is regulated by fetal urine-derived stimulators and AF inhibitors. Our objective was to utilize a multiomics approach to determine the IM transport pathways and identify the regulators. Four groups of fetal sheep with experimentally induced alterations in IM transport rate were studied: control, urine drainage (UD), urine drainage with fluid replacement (UDR), and intra-amniotic fluid infusion (IA). Amnion, AF, and fetal urine were subjected to transc

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Toth, Andrea E., Mikkel R. Holst, and Morten S. Nielsen. "Vesicular Transport Machinery in Brain Endothelial Cells: What We Know and What We Do not." Current Pharmaceutical Design 26, no. 13 (2020): 1405–16. http://dx.doi.org/10.2174/1381612826666200212113421.

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The vesicular transport machinery regulates numerous essential functions in cells such as cell polarity, signaling pathways, and the transport of receptors and their cargoes. From a pharmaceutical perspective, vesicular transport offers avenues to facilitate the uptake of therapeutic agents into cells and across cellular barriers. In order to improve receptor-mediated transcytosis of biologics across the blood-brain barrier and into the diseased brain, a detailed understanding of intracellular transport mechanisms is essential. The vesicular transport machinery is a highly complex network and

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Schwaninger, R., H. Plutner, G. M. Bokoch, and W. E. Balch. "Multiple GTP-binding proteins regulate vesicular transport from the ER to Golgi membranes." Journal of Cell Biology 119, no. 5 (1992): 1077–96. http://dx.doi.org/10.1083/jcb.119.5.1077.

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Using indirect immunofluorescence we have examined the effects of reagents which inhibit the function of ras-related rab small GTP-binding proteins and heterotrimeric G alpha beta gamma proteins in ER to Golgi transport. Export from the ER was inhibited by an antibody towards rab1B and an NH2-terminal peptide which inhibits ARF function (Balch, W. E., R. A. Kahn, and R. Schwaninger. 1992. J. Biol. Chem. 267:13053-13061), suggesting that both of these small GTP-binding proteins are essential for the transport vesicle formation. Export from the ER was also potently inhibited by mastoparan, a pep

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Drin, Guillaume, Joachim Moser von Filseck, and Alenka Čopič. "New molecular mechanisms of inter-organelle lipid transport." Biochemical Society Transactions 44, no. 2 (2016): 486–92. http://dx.doi.org/10.1042/bst20150265.

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Lipids are precisely distributed in cell membranes, along with associated proteins defining organelle identity. Because the major cellular lipid factory is the endoplasmic reticulum (ER), a key issue is to understand how various lipids are subsequently delivered to other compartments by vesicular and non-vesicular transport pathways. Efforts are currently made to decipher how lipid transfer proteins (LTPs) work either across long distances or confined to membrane contact sites (MCSs) where two organelles are at close proximity. Recent findings reveal that proteins of the oxysterol-binding prot

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Heinrich, Reinhart, and Tom A. Rapoport. "Generation of nonidentical compartments in vesicular transport systems." Journal of Cell Biology 168, no. 2 (2005): 271–80. http://dx.doi.org/10.1083/jcb.200409087.

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How can organelles communicate by bidirectional vesicle transport and yet maintain different protein compositions? We show by mathematical modeling that a minimal system, in which the basic variables are cytosolic coats for vesicle budding and membrane-bound soluble N-ethyl-maleimide–sensitive factor attachment protein receptors (SNAREs) for vesicle fusion, is sufficient to generate stable, nonidentical compartments. A requirement for establishing and maintaining distinct compartments is that each coat preferentially packages certain SNAREs during vesicle budding. Vesicles fuse preferentially

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Horenkamp, Florian A., Shaeri Mukherjee, Eric Alix, et al. "Legionella pneumophilaSubversion of Host Vesicular Transport by SidC Effector Proteins." Traffic 15, no. 5 (2014): 488–99. http://dx.doi.org/10.1111/tra.12158.

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Lev, Sima. "Non-vesicular lipid transport by lipid-transfer proteins and beyond." Nature Reviews Molecular Cell Biology 11, no. 10 (2010): 739–50. http://dx.doi.org/10.1038/nrm2971.

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Zhang, Tao, Siew Heng Wong, Bor Luen Tang, Yue Xu, and Wanjin Hong. "Morphological and Functional Association of Sec22b/ERS-24 with the pre-Golgi Intermediate Compartment." Molecular Biology of the Cell 10, no. 2 (1999): 435–53. http://dx.doi.org/10.1091/mbc.10.2.435.

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Yeast Sec22p participates in both anterograde and retrograde vesicular transport between the endoplasmic reticulum (ER) and the Golgi apparatus by functioning as a v-SNARE (solubleN-ethylmaleimide-sensitive factor [NSF] attachment protein receptor) of transport vesicles. Three mammalian proteins homologous to Sec22p have been identified and are referred to as Sec22a, Sec22b/ERS-24, and Sec22c, respectively. The existence of three homologous proteins in mammalian cells calls for detailed cell biological and functional examinations of each individual protein. The epitope-tagged forms of all thre

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Fairn, Gregory D., and Christopher R. McMaster. "The roles of the human lipid-binding proteins ORP9S and ORP10S in vesicular transport." Biochemistry and Cell Biology 83, no. 5 (2005): 631–36. http://dx.doi.org/10.1139/o05-064.

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Inactivation of the yeast oxysterol binding protein related protein (ORP) family member Kes1p allows yeast cells to survive in the absence of Sec14p, a phospholipid transfer protein required for cell viability because of the role it plays in transporting vesicles from the Golgi. We expressed human ORP9S and ORP10S in yeast lacking Sec14p and Kes1p function, and found that ORP9S completely complemented Kes1p function, whereas ORP10S possessed only a weak ability to replace Kes1p function. Purified ORP9S protein bound several phosphoinositides, whereas ORP10 bound specifically to phosphatidylino

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Xiao, Xu, Youngjae Kim, Beatriz Romartinez-Alonso, et al. "Selective Aster inhibitors distinguish vesicular and nonvesicular sterol transport mechanisms." Proceedings of the National Academy of Sciences 118, no. 2 (2020): e2024149118. http://dx.doi.org/10.1073/pnas.2024149118.

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The Aster proteins (encoded by the Gramd1a-c genes) contain a ligand-binding fold structurally similar to a START domain and mediate nonvesicular plasma membrane (PM) to endoplasmic reticulum (ER) cholesterol transport. In an effort to develop small molecule modulators of Asters, we identified 20α-hydroxycholesterol (HC) and U18666A as lead compounds. Unfortunately, both 20α-HC and U18666A target other sterol homeostatic proteins, limiting their utility. 20α-HC inhibits sterol regulatory element-binding protein 2 (SREBP2) processing, and U18666A is an inhibitor of the vesicular trafficking pro

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Ayala, S. J. "Transport and internal organization of membranes: vesicles, membrane networks and GTP-binding proteins." Journal of Cell Science 107, no. 4 (1994): 753–63. http://dx.doi.org/10.1242/jcs.107.4.753.

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Eukaryotic cells contain a variety of membranous organelles such as the Golgi complex and endosomes, which are organized to allow the flow of molecules to specific regions within the cell. Well known examples of this targeted flow include the transport of specific molecules to the apical pole of epithelial cells, to the axon terminals of neurons, and the transcytosis of immunoglobulins. The generally accepted model of transport between the different intracellular compartments maintains that transport is mediated by carrier vesicles, but recent data show the participation of tubulovesicular str

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Giordano, Francesca. "Non-vesicular lipid trafficking at the endoplasmic reticulum–mitochondria interface." Biochemical Society Transactions 46, no. 2 (2018): 437–52. http://dx.doi.org/10.1042/bst20160185.

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Mitochondria are highly dynamic organelles involved in various cellular processes such as energy production, regulation of calcium homeostasis, lipid trafficking, and apoptosis. To fulfill all these functions and preserve their morphology and dynamic behavior, mitochondria need to maintain a defined protein and lipid composition in both their membranes. The maintenance of mitochondrial membrane identity requires a selective and regulated transport of specific lipids from/to the endoplasmic reticulum (ER) and across the mitochondria outer and inner membranes. Since they are not integrated in th

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Raychaudhuri, S., and W. A. Prinz. "Uptake and trafficking of exogenous sterols in Saccharomyces cerevisiae." Biochemical Society Transactions 34, no. 3 (2006): 359–62. http://dx.doi.org/10.1042/bst0340359.

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The proper distribution of sterols among organelles is critical for numerous cellular functions. How sterols are sorted and moved among membranes remains poorly understood, but they are transported not only in vesicles but also by non-vesicular pathways. One of these pathways moves exogenous sterols from the plasma membrane to the endoplasmic reticulum in the yeast Saccharomyces cerevisiae. We have found that two classes of proteins play critical roles in this transport, ABC transporters (ATP-binding-cassette transporters) and oxysterol-binding protein-related proteins. Transport is also regul

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Guan, J. L., A. Ruusala, H. Cao, and J. K. Rose. "Effects of altered cytoplasmic domains on transport of the vesicular stomatitis virus glycoprotein are transferable to other proteins." Molecular and Cellular Biology 8, no. 7 (1988): 2869–74. http://dx.doi.org/10.1128/mcb.8.7.2869.

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Alterations of the cytoplasmic domain of the vesicular stomatitis virus glycoprotein (G protein) were shown previously to affect transport of the protein from the endoplasmic reticulum, and recent studies have shown that this occurs without detectable effects on G protein folding and trimerization (R. W. Doms et al., J. Cell Biol., in press). Deletions within this domain slowed exit of the mutant proteins from the endoplasmic reticulum, and replacement of this domain with a foreign 12-amino-acid sequence blocked all transport out of the endoplasmic reticulum. To extend these studies, we determ

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Guan, J. L., A. Ruusala, H. Cao, and J. K. Rose. "Effects of altered cytoplasmic domains on transport of the vesicular stomatitis virus glycoprotein are transferable to other proteins." Molecular and Cellular Biology 8, no. 7 (1988): 2869–74. http://dx.doi.org/10.1128/mcb.8.7.2869-2874.1988.

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Alterations of the cytoplasmic domain of the vesicular stomatitis virus glycoprotein (G protein) were shown previously to affect transport of the protein from the endoplasmic reticulum, and recent studies have shown that this occurs without detectable effects on G protein folding and trimerization (R. W. Doms et al., J. Cell Biol., in press). Deletions within this domain slowed exit of the mutant proteins from the endoplasmic reticulum, and replacement of this domain with a foreign 12-amino-acid sequence blocked all transport out of the endoplasmic reticulum. To extend these studies, we determ

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Zhang, Fan, Naseem A. Gaur, Jiri Hasek, et al. "Disrupting Vesicular Trafficking at the Endosome Attenuates Transcriptional Activation by Gcn4." Molecular and Cellular Biology 28, no. 22 (2008): 6796–818. http://dx.doi.org/10.1128/mcb.00800-08.

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ABSTRACT The late endosome (MVB) plays a key role in coordinating vesicular transport of proteins between the Golgi complex, vacuole/lysosome, and plasma membrane. We found that deleting multiple genes involved in vesicle fusion at the MVB (class C/D vps mutations) impairs transcriptional activation by Gcn4, a global regulator of amino acid biosynthetic genes, by decreasing the ability of chromatin-bound Gcn4 to stimulate preinitiation complex assembly at the promoter. The functions of hybrid activators with Gal4 or VP16 activation domains are diminished in class D mutants as well, suggesting

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Yoshida, Kazuya, Takeshi Matsui, and Atsuhiko Shinmyo. "The plant vesicular transport engineering for production of useful recombinant proteins." Journal of Molecular Catalysis B: Enzymatic 28, no. 4-6 (2004): 167–71. http://dx.doi.org/10.1016/j.molcatb.2004.01.017.

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Clary, D. O., and J. E. Rothman. "Purification of three related peripheral membrane proteins needed for vesicular transport." Journal of Biological Chemistry 265, no. 17 (1990): 10109–17. http://dx.doi.org/10.1016/s0021-9258(19)38786-1.

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Rexach, Michael, Christophe d'Enfert, Linda Wuestehube, and Randy Schekman. "Genes and proteins required for vesicular transport from the endoplasmic reticulum." Antonie van Leeuwenhoek 61, no. 2 (1992): 87–92. http://dx.doi.org/10.1007/bf00580612.

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SIMONS, MATIAS, RAINER SAFFRICH, JOCHEN REISER, and PETER MUNDEL. "Directed Membrane Transport Is Involved in Process Formation in Cultured Podocytes." Journal of the American Society of Nephrology 10, no. 8 (1999): 1633–39. http://dx.doi.org/10.1681/asn.v1081633.

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Abstract. Mature glomerular visceral epithelial cells, or podocytes, are unique cells with a complex cell architecture. Characteristically, they possess a highly branched array of major processes and foot processes, which are essential for glomerular filtration in the kidney. A podocyte cell line with the potential to exhibit many features of differentiated podocytes, particularly the formation of cell processes, was recently established. In this study, it is shown that directed membrane transport is involved in process formation in cultured podocytes. The well-characterized vesicular stomatit

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Nickel, Walter, Britta Brügger, and Felix T. Wieland. "Vesicular transport: the core machinery of COPI recruitment and budding." Journal of Cell Science 115, no. 16 (2002): 3235–40. http://dx.doi.org/10.1242/jcs.115.16.3235.

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Vesicular transport is the predominant mechanism for exchange of proteins and lipids between membrane-bound organelles in eukaryotic cells. Golgi-derived COPI-coated vesicles are involved in several vesicular transport steps, including bidirectional transport within the Golgi and recycling to the ER. Recent work has shed light on the mechanism of COPI vesicle biogenesis, in particular the machinery required for vesicle formation. The new findings have allowed us to generate a model that covers the cycle of coat recruitment, coat polymerization, vesicle budding and uncoating.

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Chamberlain, Luke H., Kimon Lemonidis, Maria Sanchez-Perez, Martin W. Werno, Oforiwa A. Gorleku, and Jennifer Greaves. "Palmitoylation and the trafficking of peripheral membrane proteins." Biochemical Society Transactions 41, no. 1 (2013): 62–66. http://dx.doi.org/10.1042/bst20120243.

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Palmitoylation, the attachment of palmitate and other fatty acids on to cysteine residues, is a common post-translational modification of both integral and peripheral membrane proteins. Dynamic palmitoylation controls the intracellular distribution of peripheral membrane proteins by regulating membrane–cytosol exchange and/or by modifying the flux of the proteins through vesicular transport systems.

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LeBlanc, Marissa A., and Christopher R. McMaster. "Surprising roles for phospholipid binding proteins revealed by high throughput geneticsThis paper is one of a selection of papers published in this special issue entitled “Second International Symposium on Recent Advances in Basic, Clinical, and Social Medicine” and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 88, no. 4 (2010): 565–74. http://dx.doi.org/10.1139/o09-171.

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Saccharomyces cerevisiae remains an ideal organism for studying the cell biological roles of lipids in vivo, as yeast has phospholipid metabolic pathways similar to mammalian cells, is easy and economical to manipulate, and is genetically tractable. The availability of isogenic strains containing specific genetic inactivation of each non-essential gene allowed for the development of a high-throughput method, called synthetic genetic analysis (SGA), to identify and describe precise pathways or functions associated with specific genes. This review describes the use of SGA to aid in elucidating t

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Blum, R., D. J. Stephens, and I. Schulz. "Lumenal targeted GFP, used as a marker of soluble cargo, visualises rapid ERGIC to Golgi traffic by a tubulo-vesicular network." Journal of Cell Science 113, no. 18 (2000): 3151–59. http://dx.doi.org/10.1242/jcs.113.18.3151.

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The mechanism by which soluble proteins without sorting motifs are transported to the cell surface is not clear. Here we show that soluble green fluorescent protein (GFP) targeted to the lumen of the endoplasmic reticulum but lacking any known retrieval, retention or targeting motifs, was accumulated in the lumen of the ERGIC if cells were kept at reduced temperature. Upon activation of anterograde transport by rewarming of cells, lumenal GFP stained a microtubule-dependent, pre-Golgi tubulo-vesicular network that served as transport structure between peripheral ERGIC-elements and the perinucl

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Müsch, A., H. Xu, D. Shields, and E. Rodriguez-Boulan. "Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells." Journal of Cell Biology 133, no. 3 (1996): 543–58. http://dx.doi.org/10.1083/jcb.133.3.543.

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Current model propose that in nonpolarized cells, transport of plasma membrane proteins to the surface occurs by default. In contrast, compelling evidence indicates that in polarized epithelial cells, plasma membrane proteins are sorted in the TGN into at least two vectorial routes to apical and basolateral surface domains. Since both apical and basolateral proteins are also normally expressed by both polarized and nonpolarized cells, we explored here whether recently described basolateral sorting signals in the cytoplasmic domain of basolateral proteins are recognized and used for post TGN tr

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Kamada, Yoshiaki, Tomoko Funakoshi, Takahiro Shintani, Kazuya Nagano, Mariko Ohsumi, and Yoshinori Ohsumi. "Tor-Mediated Induction of Autophagy via an Apg1 Protein Kinase Complex." Journal of Cell Biology 150, no. 6 (2000): 1507–13. http://dx.doi.org/10.1083/jcb.150.6.1507.

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Autophagy is a membrane trafficking to vacuole/lysosome induced by nutrient starvation. In Saccharomyces cerevisiae, Tor protein, a phosphatidylinositol kinase-related kinase, is involved in the repression of autophagy induction by a largely unknown mechanism. Here, we show that the protein kinase activity of Apg1 is enhanced by starvation or rapamycin treatment. In addition, we have also found that Apg13, which binds to and activates Apg1, is hyperphosphorylated in a Tor-dependent manner, reducing its affinity to Apg1. This Apg1–Apg13 association is required for autophagy, but not for the cyt

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Wooding, Steven, and Hugh R. B. Pelham. "The Dynamics of Golgi Protein Traffic Visualized in Living Yeast Cells." Molecular Biology of the Cell 9, no. 9 (1998): 2667–80. http://dx.doi.org/10.1091/mbc.9.9.2667.

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We describe for the first time the visualization of Golgi membranes in living yeast cells, using green fluorescent protein (GFP) chimeras. Late and early Golgi markers are present in distinct sets of scattered, moving cisternae. The immediate effects of temperature-sensitive mutations on the distribution of these markers give clues to the transport processes occurring. We show that the late Golgi marker GFP-Sft2p and the glycosyltransferases, Anp1p and Mnn1p, disperse into vesicle-like structures within minutes of a temperature shift insec18, sft1, and sed5cells, but not in sec14 cells. This i

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Aridor, M., S. I. Bannykh, T. Rowe, and W. E. Balch. "Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport." Journal of Cell Biology 131, no. 4 (1995): 875–93. http://dx.doi.org/10.1083/jcb.131.4.875.

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COPI and COPII are vesicle coat complexes whose assembly is regulated by the ARF1 and Sar1 GTPases, respectively. We show that COPI and COPII coat complexes are recruited separately and independently to ER (COPII), pre-Golgi (COPI, COPII), and Golgi (COPI) membranes of mammalian cells. To address their individual roles in ER to Golgi transport, we used stage specific in vitro transport assays to synchronize movement of cargo to and from pre-Golgi intermediates, and GDP- and GTP-restricted forms of Sar1 and ARF1 proteins to control coat recruitment. We find that COPII is solely responsible for

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Kunduri, Govind, Changqing Yuan, Velayoudame Parthibane, et al. "Phosphatidic acid phospholipase A1 mediates ER–Golgi transit of a family of G protein–coupled receptors." Journal of Cell Biology 206, no. 1 (2014): 79–95. http://dx.doi.org/10.1083/jcb.201405020.

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The coat protein II (COPII)–coated vesicular system transports newly synthesized secretory and membrane proteins from the endoplasmic reticulum (ER) to the Golgi complex. Recruitment of cargo into COPII vesicles requires an interaction of COPII proteins either with the cargo molecules directly or with cargo receptors for anterograde trafficking. We show that cytosolic phosphatidic acid phospholipase A1 (PAPLA1) interacts with COPII protein family members and is required for the transport of Rh1 (rhodopsin 1), an N-glycosylated G protein–coupled receptor (GPCR), from the ER to the Golgi complex

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Springer, S., E. Chen, R. Duden, et al. "The p24 proteins are not essential for vesicular transport in Saccharomyces cerevisiae." Proceedings of the National Academy of Sciences 97, no. 8 (2000): 4034–39. http://dx.doi.org/10.1073/pnas.070044097.

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Liu and, Yongjian, and Robert H. Edwards. "THE ROLE OF VESICULAR TRANSPORT PROTEINS IN SYNAPTIC TRANSMISSION AND NEURAL DEGENERATION." Annual Review of Neuroscience 20, no. 1 (1997): 125–56. http://dx.doi.org/10.1146/annurev.neuro.20.1.125.

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Chakraborty, Paramita, Per Bjork, Eva Källberg, et al. "Vesicular Location and Transport of S100A8 and S100A9 Proteins in Monocytoid Cells." PLOS ONE 10, no. 12 (2015): e0145217. http://dx.doi.org/10.1371/journal.pone.0145217.

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Péchoux, Christine, Raphaël Boisgard, Eric Chanat, and Françoise Lavialle. "Ca2+-independent phospholipase A2 participates in the vesicular transport of milk proteins." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1743, no. 3 (2005): 317–29. http://dx.doi.org/10.1016/j.bbamcr.2005.01.006.

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Teves, Maria, Eduardo Roldan, Diego Krapf, Jerome Strauss III, Virali Bhagat, and Paulene Sapao. "Sperm Differentiation: The Role of Trafficking of Proteins." International Journal of Molecular Sciences 21, no. 10 (2020): 3702. http://dx.doi.org/10.3390/ijms21103702.

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Sperm differentiation encompasses a complex sequence of morphological changes that takes place in the seminiferous epithelium. In this process, haploid round spermatids undergo substantial structural and functional alterations, resulting in highly polarized sperm. Hallmark changes during the differentiation process include the formation of new organelles, chromatin condensation and nuclear shaping, elimination of residual cytoplasm, and assembly of the sperm flagella. To achieve these transformations, spermatids have unique mechanisms for protein trafficking that operate in a coordinated fashi

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Mundy, D. I., and G. Warren. "Mitosis and inhibition of intracellular transport stimulate palmitoylation of a 62-kD protein." Journal of Cell Biology 116, no. 1 (1992): 135–46. http://dx.doi.org/10.1083/jcb.116.1.135.

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Recent studies suggest that a cycle of acylation/deacylation is involved in the vesicular transport of proteins between intracellular compartments at both the budding and the fusion stage (Glick, B. S., and J. E. Rothman. 1987. Nature (Lond.). 326:309-312). Since a number of cellular processes requiring vesicular transport are inhibited during mitosis, we examined the fatty acylation of proteins in interphase and mitotic cells. We have identified a major palmitoylated protein with an apparent molecular weight of 62,000 (p62), whose level of acylation increases 5-10-fold during mitosis. Acylati

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Maxfield, Frederick R., David B. Iaea, and Nina H. Pipalia. "Role of STARD4 and NPC1 in intracellular sterol transport." Biochemistry and Cell Biology 94, no. 6 (2016): 499–506. http://dx.doi.org/10.1139/bcb-2015-0154.

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Cholesterol plays an important role in determining the biophysical properties of membranes in mammalian cells, and the concentration of cholesterol in membranes is tightly regulated. Cholesterol moves among membrane organelles by a combination of vesicular and nonvesicular transport pathways, but the details of these transport pathways are not well understood. In this review, we discuss the mechanisms for nonvesicular sterol transport with an emphasis on the role of STARD4, a small, soluble, cytoplasmic sterol transport protein. STARD4 can rapidly equilibrate sterol between membranes, especial

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