The Vesicle Docking Protein p115 Binds GM130, a cis-Golgi Matrix Protein, in a Mitotically Regulated Manner

Nakamura, Nobuhiro; Lowe, Martin; Levine, Tim P.; Rabouille, Cathérine; Warren, Graham

doi:10.1016/s0092-8674(00)80225-1

Cited by 391 publications

(442 citation statements)

References 26 publications

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“…[91][92][93] The very C-terminus of GM130 may bind to and stimulate the catalytic activity of HtrA1, a serine protease that inhibits TGF-b signaling. 94 EspG proteins produced by enteric pathogens may interact with GM130 and disrupt protein secretion of the host cells.…”

Section: Gcks In Immune Regulationmentioning

confidence: 99%

Germinal center kinases in immune regulation

Yin

Shi

et al. 2012

Cell Mol Immunol

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Section: Gcks In Immune Regulationmentioning

confidence: 99%

Germinal center kinases in immune regulation

Yin

Shi

et al. 2012

Cell Mol Immunol

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“…GM130 is a cis-Golgi localized coiled-coil protein targeted to membranes via the peripheral membrane protein GRASP65 (Barr et al, 1997(Barr et al, , 1998. It also binds the vesicle tethering factor p115 (Nakamura et al, 1997;Nelson et al, 1998). GM130 and GRASP65 are key determinants for maintaining Golgi morphology as their knockdown transforms the Golgi ribbon to mini-stacks (Sohda et al, 2005;Puthenveedu et al, 2006).…”

Section: Golgi Matrix Proteins Remain Associated With the Dispersed Gmentioning

confidence: 99%

The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi

Mitrović

Ben-Tekaya

Koegler

et al. 2008

MBoC

115

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Rapidly cycling proteins of the early secretory pathway can operate as cargo receptors. Known cargo receptors are abundant proteins, but it remains mysterious why their inactivation leads to rather limited secretion phenotypes. Studies of Surf4, the human orthologue of the yeast cargo receptor Erv29p, now reveal a novel function of cargo receptors. Surf4 was found to interact with endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53 and p24 proteins. Silencing Surf4 together with ERGIC-53 or silencing the p24 family member p25 induced an identical phenotype characterized by a reduced number of ERGIC clusters and fragmentation of the Golgi apparatus without effect on anterograde transport. Live imaging showed decreased stability of ERGIC clusters after knockdown of p25. Silencing of Surf4/ERGIC-53 or p25 resulted in partial redistribution of coat protein (COP) I but not Golgi matrix proteins to the cytosol and partial resistance of the cis-Golgi to brefeldin A. These findings imply that cargo receptors are essential for maintaining the architecture of ERGIC and Golgi by controlling COP I recruitment. INTRODUCTIONThe secretory pathway of higher eukaryotic cells is composed of the three membrane organelles endoplasmic reticulum (ER), ER-Golgi intermediate compartment (ERGIC), and Golgi (Bonifacino and Glick, 2004;Appenzeller-Herzog and Hauri, 2006). Maintenance of these organelles requires a balance of anterograde (secretory) and retrograde vesicular traffic. Anterograde traffic from ER to ERGIC is mediated by coat protein (COP) II vesicles that form at ER exit sites (Aridor et al., 1995;Zeuschner et al., 2006) and fuse with the ERGIC that consists of a few hundred tubulovesicular membrane clusters in vicinity of ER exit sites (AppenzellerHerzog and Hauri, 2006). Transport from ERGIC to Golgi is mediated by pleomorphic vesicles (Ben-Tekaya et al., 2005) that carry COP I (Presley et al., 1997;Scales et al., 1997), although the mechanism of their formation remains unknown. Retrograde traffic mediated by COP I vesicles can occur from ERGIC or Golgi and recycles membrane proteins that possess either dilysine signals, including ERGIC-53 and KDEL-receptor, or diphenylalanine signals, such as members of the 24 protein family. This rapid COP I-dependent recycling is distinct from the slow Golgi-to-ER recycling of Golgi resident proteins that is COP I independent and can be either constitutive or induced (Storrie, 2005).Major constituents of anterograde and retrograde transport vesicles are transmembrane cargo receptors that mediate protein sorting by linking soluble cargo on the luminal side and coat assembly on the cytoplasmic side. To date, only few cargo receptors have been studied in detail. The polytopic transmembrane protein Erv29p is known to cycle between ER and Golgi in yeast and to operate as a cargo receptor (Belden and Barlowe, 2001). Erv29p is required for efficient packaging of the glycosylated ␣-factor pheromone precursor into COP II vesicles departing from the ER. Maturation of carboxypeptidase Y...

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“…Alternatively, the Vps52/53/54 complex could be required to maintain the integrity of the TGN. The two possibilities are not mutually exclusive: GM130 functions both as a docking factor, interacting with p115 in intra-Golgi transport in mammalian cells, and as a matrix protein, mediating the assembly and disassembly of stacked Golgi cisternae through successive cell divisions coupled to a cycle of phosphorylation/dephosphorylation (Nakamura et al, 1997;Lowe et al, 1998). The isolation of temperature-sensitive-forfunction alleles of vps52, vps53, and vps54 should help in separating the direct effects of these mutations from those resulting from long-term loss of late Golgi function.…”

Section: Function Of the Vps52/53/54 Complex In Golgi Sortingmentioning

confidence: 99%

“…The multisubunit TRAPP complex, which is found on the cis Golgi and also acts in ER-to-Golgi transport at a step preceding SNARE complex assembly, shows genetic interactions with Uso1p and Ypt1p and may also participate in vesicle docking (Sacher et al, 1998). The mammalian homologue of Uso1p, p115, acts as a docking factor to link the vesicle-associated protein giantin with a complex of GM130 and GRASP65 on Golgi membranes during intra-Golgi transport (Nakamura et al, 1997;Sonnichsen et al, 1998). In addition, the endosomal protein EEA1 binds Rab5 and is important for endosome docking in the homotypic fusion of early endosomes (Christoforidis et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Vps52p, Vps53p, and Vps54p Form a Novel Multisubunit Complex Required for Protein Sorting at the Yeast Late Golgi

Conibear

Stevens

2000

MBoC

266

336

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The late Golgi of the yeast Saccharomyces cerevisiae receives membrane traffic from the secretory pathway as well as retrograde traffic from post-Golgi compartments, but the machinery that regulates these vesicle-docking and fusion events has not been characterized. We have identified three components of a novel protein complex that is required for protein sorting at the yeast late Golgi compartment. Mutation of VPS52, VPS53, or VPS54 results in the missorting of 70% of the vacuolar hydrolase carboxypeptidase Y as well as the mislocalization of late Golgi membrane proteins to the vacuole, whereas protein traffic through the early part of the Golgi complex is unaffected. A vps52/53/54 triple mutant strain is phenotypically indistinguishable from each of the single mutants, consistent with the model that all three are required for a common step in membrane transport. Native coimmunoprecipitation experiments indicate that Vps52p, Vps53p, and Vps54p are associated in a 1:1:1 complex that sediments as a single peak on sucrose velocity gradients. This complex, which exists both in a soluble pool and as a peripheral component of a membrane fraction, colocalizes with markers of the yeast late Golgi by immunofluorescence microscopy. Together, the phenotypic and biochemical data suggest that VPS52, VPS53, and VPS54 are required for the retrograde transport of Golgi membrane proteins from an endosomal/ prevacuolar compartment. The Vps52/53/54 complex joins a growing list of distinct multisubunit complexes that regulate membrane-trafficking events.

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The Vesicle Docking Protein p115 Binds GM130, a cis-Golgi Matrix Protein, in a Mitotically Regulated Manner

Cited by 391 publications

References 26 publications

Germinal center kinases in immune regulation

Germinal center kinases in immune regulation

The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi

Vps52p, Vps53p, and Vps54p Form a Novel Multisubunit Complex Required for Protein Sorting at the Yeast Late Golgi

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