Domains within the GARP Subunit Vps54 Confer Separate Functions in Complex Assembly and Early Endosome Recognition

Quenneville, Nicole R.; Chao, Tzu‐Yuan; McCaffery, J. Michael; Conibear, Elizabeth

doi:10.1091/mbc.e05-11-1002

Cited by 43 publications

(60 citation statements)

References 56 publications

(87 reference statements)

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“…The TRAPPII complex is thought to reside on the TGN and to tether Golgi-derived as well as endocytotic vesicles in yeast (Cai et al, 2005). The GARP complex is also thought to reside on the TGN, where it tethers early (large, red) and late (small, white) endocytotic vesicles (Conibear et al, 2003;Quenneville et al, 2006). From the trans-Golgi, secretion to the plasma membrane would be mediated by the Exocyst complex, whereas vesicles destined for the prevacuolar compartment and the vacuole would be tethered by the HOPS (or VPS) complex.…”

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confidence: 99%

“…We focused on the TRAPPI, TRAPPII, and GARP tethering complexes because they mediate the flow of traffic through the Golgi apparatus and from the cell surface. Both the TRAPPII and GARP complexes have been shown to reside on the TGN in yeast (Conibear et al, 2003;Cai et al, 2005;Quenneville et al, 2006). Whereas the TRAPPII complex is required for both exocytosis and endocytosis, the GARP complex has only been implicated in endocytosis (Conibear et al, 2003;Cai et al, 2005;Quenneville et al, 2006).…”

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“…Both the TRAPPII and GARP complexes have been shown to reside on the TGN in yeast (Conibear et al, 2003;Cai et al, 2005;Quenneville et al, 2006). Whereas the TRAPPII complex is required for both exocytosis and endocytosis, the GARP complex has only been implicated in endocytosis (Conibear et al, 2003;Cai et al, 2005;Quenneville et al, 2006). The TGN has been shown to function as an early endosome in plants (Dettmer et al, 2006;Lam et al, 2007;Wang et al, 2010).…”

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Tethering Factors Required for Cytokinesis in Arabidopsis

et al. 2010

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At the end of the cell cycle, the nascent cross wall is laid down within a transient membrane compartment referred to as the cell plate. Tethering factors, which act by capturing vesicles and holding them in the vicinity of their target membranes, are likely to play an important role in the first stages of cell plate assembly. Factors required for cell plate biogenesis, however, remain to be identified. In this study, we used a reverse genetic screen to isolate tethering factors required for cytokinesis in Arabidopsis (Arabidopsis thaliana). We focused on the TRAPPI and TRAPPII (for transport protein particle) tethering complexes, which are thought to be required for the flow of traffic through the Golgi and for trans-Golgi network function, as well as on the GARP complex, thought to be required for the tethering of endocytotic vesicles to the trans-Golgi network. We found weak cytokinesis defects in some TRAPPI mutants and strong cytokinesis defects in all the TRAPPII lines we surveyed. Indeed, four insertion lines at the TRAPPII locus AtTRS120 had canonical cytokinesis-defective seedling-lethal phenotypes, including cell wall stubs and incomplete cross walls. Confocal and electron microscopy showed that in trs120 mutants, vesicles accumulated at the equator of dividing cells yet failed to assemble into a cell plate. This shows that AtTRS120 is required for cell plate biogenesis. In contrast to the TRAPP complexes, we found no conclusive evidence for cytokinesis defects in seven GARP insertion lines. We discuss the implications of these findings for the origin and identity of cell plate membranes.

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Tethering Factors Required for Cytokinesis in Arabidopsis

et al. 2010

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“…To distinguish between these possibilities, we first determined if Dtr1p expressed in vegetative cells is recycled via the endosome. To that end, we examined the localization of CLB2 promoter-driven Dtr1p-GFP in the vps54⌬ mutant; Vps54p is a component of the GARP tethering complex that is involved in recycling membrane proteins such as the v-SNARE Snc1p (33). Dtr1p-GFP localized to the PM and vacuoles in vps54⌬ cells, similar to the case for wild-type cells, suggesting that Dtr1p-GFP is not recycled through the endosome in a GARPdependent manner (Fig.…”

Section: Vol 7 2008mentioning

confidence: 77%

Sorting Signals within the Saccharomyces cerevisiae Sporulation-Specific Dityrosine Transporter, Dtr1p, C Terminus Promote Golgi-to-Prospore Membrane Transport

Morishita

Engebrecht

2008

Eukaryot Cell

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During sporulation in Saccharomyces cerevisiae, the dityrosine transporter Dtr1p, which is required for formation of the outermost layer of the spore wall, is specifically expressed and transported to the prospore membrane, a novel double-lipid-bilayer membrane. Dtr1p consists of 572 amino acids with predicted N-and C-terminal cytoplasmic extensions and 12 transmembrane domains. Dtr1p missing the largest internal cytoplasmic loop was trapped in the endoplasmic reticulum in both mitotically dividing cells and cells induced to sporulate. Deletion of the carboxyl 15 amino acids, but not the N-terminal extension of Dtr1p, resulted in a protein that failed to localize to the prospore membrane and was instead observed in cytoplasmic puncta. The puncta colocalized with a cis-Golgi marker, suggesting that Dtr1p missing the last 15 amino acids was trapped in an early Golgi compartment. Deletion of the C-terminal 10 amino acids resulted in a protein that localized to the prospore membrane with a delay and accumulated in cytoplasmic puncta that partially colocalized with a trans-Golgi marker. Both full-length Dtr1p and Dtr1p missing the last 10 amino acids expressed in vegetative cells localized to the plasma membrane and vacuoles, while Dtr1p deleted for the carboxyl-terminal 15 amino acids was observed only at vacuoles, suggesting that transport to the prospore membrane is mediated by distinct signals from those that specify plasma membrane localization. Transfer-of-function experiments revealed that both the carboxyl transmembrane domain and the C-terminal tail are important for Golgi complex-to-prospore membrane transport.Saccharomyces cerevisiae sporulation is a complex sexual differentiation program initiated in MATa/MAT␣ diploid cells by depletion of nitrogen in the presence of a nonfermentable carbon source (16). During sporulation, four haploid gametes, packaged as spores, are produced within the mother cell to form the ascus. Sporulation requires that meiosis, the process whereby the ploidy is reduced, and spore formation be exquisitely coordinated to ensure the production of viable gametes. During the second meiotic division, new proteinaceous structures termed the meiotic outer plaques (MOPs) are formed on the cytoplasmic face of the spindle pole bodies (SPBs), which are analogous to vertebrate centrosomes, and serve as platforms for vesicles to dock and fuse to form a novel double-lipid bilayer, the prospore membrane (PSM) (12,14). PSMs develop as sacs by continuous fusion of vesicles to engulf each daughter nucleus, followed by PSM closure at the opposite side of each SPB (29). The inner lipid bilayer of the PSM becomes the plasma membrane (PM) of the spore, while the outer layer eventually lyses during the course of spore wall formation. The completion of PSM formation triggers the initiation of spore wall synthesis. The spore wall is composed of four distinct layers, namely, mannan and glucan, which form the inner layers, and chitosan and dityrosine, which form the spore-specific outer layers, formed outwar...

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“…2a) exhibits motor and sensory neurodegeneration, and carries a mutation in the phosphatase Fig 4. The substrate of Fig4, phosphatidylinositol-2,5-bisphosphate (PtdIns(3,5)P 2 ), is important to endosomal membrane trafficking [38]. Vps54 is a member of the Golgi Associated Retrograde Protein (GARP) complex, which functions in endosomal trafficking [39]; the Vps54 mutation in the wobbler (wr) strain results in motoneuron disease [40].…”

Section: Gene Discovery and Functional Analysismentioning

confidence: 99%

Mouse Forward Genetics in the Study of the Peripheral Nervous System and Human Peripheral Neuropathy

Douglas

Popko

2008

Neurochem Res

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Forward genetics, the phenotype-driven approach to investigating gene identity and function, has a long history in mouse genetics. Random mutations in the mouse transcend bias about gene function and provide avenues towards unique discoveries. The study of the peripheral nervous system is no exception; from historical strains such as the trembler mouse, which led to the identification of PMP22 as a human disease gene causing multiple forms of peripheral neuropathy, to the more recent identification of the claw paw and sprawling mutations, forward genetics has long been a tool for probing the physiology, pathogenesis, and genetics of the PNS. Even as spontaneous and mutagenized mice continue to enable the identification of novel genes, provide allelic series for detailed functional studies, and generate models useful for clinical research, new methods, such as the piggyBac transposon, are being developed to further harness the power of forward genetics.

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Domains within the GARP Subunit Vps54 Confer Separate Functions in Complex Assembly and Early Endosome Recognition

Cited by 43 publications

References 56 publications

Tethering Factors Required for Cytokinesis in Arabidopsis

Tethering Factors Required for Cytokinesis in Arabidopsis

Sorting Signals within the Saccharomyces cerevisiae Sporulation-Specific Dityrosine Transporter, Dtr1p, C Terminus Promote Golgi-to-Prospore Membrane Transport

Mouse Forward Genetics in the Study of the Peripheral Nervous System and Human Peripheral Neuropathy

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