TRAPP I Implicated in the Specificity of Tethering in ER-to-Golgi Transport

Sacher, Michael; Barrowman, Jemima; Wang, Wei; Horecka, Joe; Zhang, Yueyi; Pypaert, Marc; Ferro‐Novick, Susan

doi:10.1016/s1097-2765(01)00190-3

Cited by 222 publications

(376 citation statements)

References 45 publications

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“…Alternatively, these proteins and the phosphoinositides generated by their action may play additional roles during meiosis. Consistent with the idea that trafficking is important for meiosis, gsg1 mutants are defective in meiotic division , and recent work has indicated that Gsg1p is the high-molecular-weight subunit of both the TRAPP I complex, involved in vesicle-mediated transport from the ER to the Golgi, and the TRAPP II complex, involved in intra-Golgi trafficking (Sacher et al, 2000(Sacher et al, , 2001. Mutations in SPO15/VPS1, which encodes a dynamin-like protein required for sorting of proteins from the Golgi to the vacuole, also fail to undergo meiotic division (Yeh et al, 1991).…”

Section: Phosphoinositide Function During Meiosismentioning

confidence: 68%

Roles of Phosphoinositides and of Spo14p (phospholipase D)-generated Phosphatidic Acid during Yeast Sporulation

Rudge

Sciorra

Iwamoto

et al. 2004

MBoC

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During yeast sporulation, internal membrane synthesis ensures that each haploid nucleus is packaged into a spore. Prospore membrane formation requires Spo14p, a phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P 2 ]-stimulated phospholipase D (PLD), which hydrolyzes phosphatidylcholine (PtdCho) to phosphatidic acid (PtdOH) and choline. We found that both meiosis and spore formation also require the phosphatidylinositol (PtdIns)/PtdCho transport protein Sec14p. Specific ablation of the PtdIns transport activity of Sec14p was sufficient to impair spore formation but not meiosis. Overexpression of Pik1p, a PtdIns 4-kinase, suppressed the sec14-1 meiosis and spore formation defects; conversely, pik1-ts diploids failed to undergo meiosis and spore formation. The PtdIns(4)P 5-kinase, Mss4p, also is essential for spore formation. Use of phosphoinositide-specific GFP-PH domain reporters confirmed that PtdIns(4,5)P 2 is enriched in prospore membranes. sec14, pik1, and mss4 mutants displayed decreased Spo14p PLD activity, whereas absence of Spo14p did not affect phosphoinositide levels in vivo, suggesting that formation of PtdIns(4,5)P 2 is important for Spo14p activity. Spo14p-generated PtdOH appears to have an essential role in sporulation, because treatment of cells with 1-butanol, which supports Spo14p-catalyzed PtdCho breakdown but leads to production of Cho and Ptd-butanol, blocks spore formation at concentrations where the inert isomer, 2-butanol, has little effect. Thus, rather than a role for PtdOH in stimulating PtdIns(4,5)P 2 formation, our findings indicate that during sporulation, Spo14p-mediated PtdOH production functions downstream of Sec14p-, Pik1p-, and Mss4p-dependent PtdIns(4,5)P 2 synthesis.

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Section: Phosphoinositide Function During Meiosismentioning

confidence: 68%

Roles of Phosphoinositides and of Spo14p (phospholipase D)-generated Phosphatidic Acid during Yeast Sporulation

Rudge

Sciorra

Iwamoto

et al. 2004

MBoC

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“…The exocyst (sec6/8 complex), composed of eight proteins, is thought to help recruit Golgiderived vesicles to the plasma membrane at the final step of the secretory pathway (Hsu et al, 1996;TerBush et al, 1996;Kee et al, 1997). The multisubunit TRAPP I and Vps52/ 53/54 complexes are believed to serve analogous functions during ER-to-Golgi and endosome-to-Golgi trafficking, respectively (Conibear and Stevens, 2000;Sacher et al, 2001). The eight-component mammalian conserved oligomeric Golgi (COG) complex and the homologous Sec34/35 complex in yeast have been proposed to assist in Golgi vesicle targeting VanRheenen et al, 1998;Walter et al, 1998;VanRheenen et al, 1999;Sacher et al, 2001;Whyte and Munro, 2001;Ungar et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

“…The multisubunit TRAPP I and Vps52/ 53/54 complexes are believed to serve analogous functions during ER-to-Golgi and endosome-to-Golgi trafficking, respectively (Conibear and Stevens, 2000;Sacher et al, 2001). The eight-component mammalian conserved oligomeric Golgi (COG) complex and the homologous Sec34/35 complex in yeast have been proposed to assist in Golgi vesicle targeting VanRheenen et al, 1998;Walter et al, 1998;VanRheenen et al, 1999;Sacher et al, 2001;Whyte and Munro, 2001;Ungar et al, 2002). The COG complex can stimulate intra-Golgi trafficking in vitro (Walter et al, 1998), and subunits of the Sec34/35 complex have been shown to be required for ER-to-Golgi trafficking, retrograde transport through the Golgi, and trafficking between the Golgi and endosomes (Spelbrink and Nothwehr, 1999;VanRheenen et al, 1999;Whyte and Munro, 2001).…”

Section: Introductionmentioning

confidence: 99%

TheDrosophila Cog5Homologue Is Required for Cytokinesis, Cell Elongation, and Assembly of Specialized Golgi Architecture during Spermatogenesis

Farkas

Giansanti

Gatti

et al. 2003

MBoC

108

149

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The multisubunit conserved oligomeric Golgi (COG) complex has been shown previously to be involved in Golgi function in yeast and mammalian tissue culture cells. Despite this broad conservation, several subunits, including Cog5, were not essential for growth and showed only mild effects on secretion when mutated in yeast, raising questions about what functions these COG complex subunits play in the life of the cell. Here, we show that function of the gene four way stop (fws), which encodes the Drosophila Cog5 homologue, is necessary for dramatic changes in cellular and subcellular morphology during spermatogenesis. Loss-of-function mutations in fws caused failure of cleavage furrow ingression in dividing spermatocytes and failure of cell elongation in differentiating spermatids and disrupted the formation and/or stability of the Golgibased spermatid acroblast. Consistent with the lack of a growth defect in yeast lacking Cog5, animals lacking fws function were viable, although males were sterile. Fws protein localized to Golgi structures throughout spermatogenesis. We propose that Fws may directly or indirectly facilitate efficient vesicle traffic through the Golgi to support rapid and extensive increases in cell surface area during spermatocyte cytokinesis and polarized elongation of differentiating spermatids. Our study suggests that Drosophila spermatogenesis can be an effective sensitized genetic system to uncover in vivo functions for proteins involved in Golgi architecture and/or vesicle transport.

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“…Mammalian homologues of the VFT⅐GARP complex are identified and could function similarly as tethering proteins in the trans-Golgi network (20). TRAPPI and -II are two related tethering complex that function in endoplasmic reticulum-Golgi and intra-Golgi transport and act together with Ypt1/Rab1 (21), whereas the HOPS complex (or Class C VPS complex) consisting of Vps11, Vps16, Vps18, Vps33, Vps39, and Vps41 act together with Ypt7 and SNAREs in mediating tether and fusion at the vacuole in yeast (22). The HOPS complex has been shown to function in multiple transport steps in addition to fusion at the vacuolar membrane (23)(24).…”

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confidence: 99%

The Binary Interacting Network of the Conserved Oligomeric Golgi Tethering Complex

Loh

Hong

2004

Journal of Biological Chemistry

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Several recent studies have revealed the existence of a conserved oligomeric Golgi (COG) complex consisting of several novel proteins as well as known Golgi proteins that were identified by independent approaches. The mammalian COG complex contains eight subunits: COG1/LdlBp, COG2/LdlCp, COG3/Sec34, COG4/Cod1, COG5/GTC-90/Cod4, COG6/Cod2, COG7, and COG8/Dor1. COG1, COG2, and COG7 seem structurally unique to mammalian cells, whereas the other five subunits are structurally conserved in yeast, which also contains three other unique proteins (COG1/Sec36p/Cod3p, COG2/Sec35p, and COG7/Cod5p). We report here the network of intermolecular interactions of the COG complex, revealed by in vitro translation and co-immunoprecipitation approaches. Our results suggest that COG4 serves as a core component of the complex by interacting directly with COG1, COG2, COG5, and COG7. COG3 is incorporated by its direct interaction with COG1 and COG2, whereas COG6 and COG8 do not interact with any individual subunit. Incorporation of COG6 into the complex depends on the concerted interaction of both COG5 and COG7, whereas optimal incorporation of COG8 depends on the concerted interaction of COG5, COG6, and COG7. Because COG4 (together with COG1, COG2, and COG3) is among the four essential genes of the COG complex in yeast, this molecular network highlights the structural basis for a crucial role of COG4 in the assembly/function of the complex. A model for the assembly of the COG complex is presented.

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TRAPP I Implicated in the Specificity of Tethering in ER-to-Golgi Transport

Cited by 222 publications

References 45 publications

Roles of Phosphoinositides and of Spo14p (phospholipase D)-generated Phosphatidic Acid during Yeast Sporulation

Roles of Phosphoinositides and of Spo14p (phospholipase D)-generated Phosphatidic Acid during Yeast Sporulation

TheDrosophila Cog5Homologue Is Required for Cytokinesis, Cell Elongation, and Assembly of Specialized Golgi Architecture during Spermatogenesis

The Binary Interacting Network of the Conserved Oligomeric Golgi Tethering Complex

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