Gene Symbol: SED5
Description: t-SNARE syntaxin
Alias: t-SNARE syntaxin
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Lupashin V, Waters M. t-SNARE activation through transient interaction with a rab-like guanosine triphosphatase. Science. 1997;276:1255-8 pubmed
    ..The data suggest that the Rab protein Ypt1p transiently interacts with the t-SNARE Sed5p and results in displacement of the negative regulator Sly1p, allowing subsequent formation of the v-SNARE-t-SNARE targeting complex. ..
  2. Grabowski R, Gallwitz D. High-affinity binding of the yeast cis-Golgi t-SNARE, Sed5p, to wild-type and mutant Sly1p, a modulator of transport vesicle docking. FEBS Lett. 1997;411:169-72 pubmed
    ..These data appear to argue for an active rather than an inhibitory role of Sly1p in vesicle docking. ..
  3. Holthuis J, Nichols B, Dhruvakumar S, Pelham H. Two syntaxin homologues in the TGN/endosomal system of yeast. EMBO J. 1998;17:113-26 pubmed
    ..However, neither is required for intra-Golgi traffic. Since no further syntaxins have been identified in yeast, this implies that the Golgi apparatus can function with a single syntaxin, Sed5p. ..
  4. Yamaguchi T, Dulubova I, Min S, Chen X, Rizo J, Sudhof T. Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Dev Cell. 2002;2:295-305 pubmed
    ..These data suggest a potentially general mechanism by which SM proteins could interact with peptides in target proteins independent of core complex assembly and suggest that munc18 binding to syntaxin is an exception. ..
  5. Søgaard M, Tani K, Ye R, Geromanos S, Tempst P, Kirchhausen T, et al. A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell. 1994;78:937-48 pubmed
  6. Tsui M, Tai W, Banfield D. Selective formation of Sed5p-containing SNARE complexes is mediated by combinatorial binding interactions. Mol Biol Cell. 2001;12:521-38 pubmed
    ..Rather our data are consistent with the existence of multiple (perhaps parallel) trafficking pathways where Sed5p-containing SNARE complexes play overlapping and/or distinct functional roles. ..
  7. McNew J, Sogaard M, Lampen N, Machida S, Ye R, Lacomis L, et al. Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi transport. J Biol Chem. 1997;272:17776-83 pubmed
    ..This is the first example of a human SNARE protein functionally replacing a yeast SNARE. This observation implies that the specific details of the vesicle targeting code, like the genetic code, are conserved in evolution. ..
  8. McNew J, Parlati F, Fukuda R, Johnston R, Paz K, Paumet F, et al. Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Nature. 2000;407:153-9 pubmed
    ..Here we find that, to a marked degree, the pattern of membrane flow in the cell is encoded and recapitulated by its isolated SNARE proteins, as predicted by the SNARE hypothesis. ..
  9. von Mollard G, Nothwehr S, Stevens T. The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p. J Cell Biol. 1997;137:1511-24 pubmed
    ..Therefore, a single v-SNARE can interact functionally with two different t-SNAREs in directing membrane traffic in yeast. ..

More Information


  1. Lupashin V, Pokrovskaya I, McNew J, Waters M. Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic. Mol Biol Cell. 1997;8:2659-76 pubmed
    ..We propose that Vti1p, along with Ykt6p and perhaps Sft1p, acts as a retrograde v-SNARE capable of interacting with the cis-Golgi t-SNARE Sed5p. ..
  2. Parlati F, McNew J, Fukuda R, Miller R, Sollner T, Rothman J. Topological restriction of SNARE-dependent membrane fusion. Nature. 2000;407:194-8 pubmed
    ..In yeast, four integral membrane proteins, Sed5, Bos1, Sec22 and Bet1 (refs 2-6), each probably contribute a single helix to form the SNARE complex that is needed ..
  3. Bracher A, Weissenhorn W. Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p. EMBO J. 2002;21:6114-24 pubmed
    ..The observed Sly1p-Sed5p interaction mode therefore indicates how SM proteins can stay associated with the assembling fusion machinery in order to participate in late fusion steps. ..
  4. Tsui M, Banfield D. Yeast Golgi SNARE interactions are promiscuous. J Cell Sci. 2000;113 ( Pt 1):145-52 pubmed
  5. Weinberger A, Kamena F, Kama R, Spang A, Gerst J. Control of Golgi morphology and function by Sed5 t-SNARE phosphorylation. Mol Biol Cell. 2005;16:4918-30 pubmed
    ..we show that the presumed phosphorylation of a conserved membrane-proximal PKA consensus site (serine-317) in the Sed5 t-SNARE regulates endoplasmic reticulum (ER)-Golgi transport, as well as Golgi morphology...
  6. Suvorova E, Duden R, Lupashin V. The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins. J Cell Biol. 2002;157:631-43 pubmed
    ..We propose that the Sec34/35 protein complex acts as a tether that connects cis-Golgi membranes and COPI-coated, retrogradely targeted intra-Golgi vesicles. ..
  7. Hardwick K, Pelham H. SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex. J Cell Biol. 1992;119:513-21 pubmed
    ..R. B. Pelham. 1990. Cell. 61:1349-1357; Lewis, M. J., D. J. Sweet, and H. R. B. Pelham. 1990. Cell. 61:1359-1363). SED5, when present in multiple copies, enables cells to grow in the absence of Erd2p...
  8. Parlati F, Varlamov O, Paz K, McNew J, Hurtado D, Sollner T, et al. Distinct SNARE complexes mediating membrane fusion in Golgi transport based on combinatorial specificity. Proc Natl Acad Sci U S A. 2002;99:5424-9 pubmed
    Syntaxin-5 (Sed5) is the only syntaxin needed for transport into and across the yeast Golgi, raising the question of how a single syntaxin species could mediate vesicle transport in both the anterograde and the retrograde direction within ..
  9. Sacher M, Stone S, Ferro Novick S. The synaptobrevin-related domains of Bos1p and Sec22p bind to the syntaxin-like region of Sed5p. J Biol Chem. 1997;272:17134-8 pubmed
  10. Coe J, Lim A, Xu J, Hong W. A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae. Mol Biol Cell. 1999;10:2407-23 pubmed
    ..Morphological analyses by electron microscopy reveal that cells depleted of Tlg1p or tlg1 ts mutants incubated at the restrictive temperature accumulate 40- to 50-nm vesicles and experience fragmentation of the vacuole. ..
  11. Wooding S, Pelham H. The dynamics of golgi protein traffic visualized in living yeast cells. Mol Biol Cell. 1998;9:2667-80 pubmed
    ..Anp1p and Mnn1p, disperse into vesicle-like structures within minutes of a temperature shift in sec18, sft1, and sed5 cells, but not in sec14 cells...
  12. McNew J, Coe J, Søgaard M, Zemelman B, Wimmer C, Hong W, et al. Gos1p, a Saccharomyces cerevisiae SNARE protein involved in Golgi transport. FEBS Lett. 1998;435:89-95 pubmed
    ..Close examination of the secretory phenotype of GOS1-disrupted cells suggests that Gos1p may play a role in multiple transport steps, specifically ER-Golgi and/or intra-Golgi transport. ..
  13. Peng R, Grabowski R, De Antoni A, Gallwitz D. Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the coat protein complex II component Sec24p of endoplasmic reticulum-derived transport vesicles. Proc Natl Acad Sci U S A. 1999;96:3751-6 pubmed
    ..Sec24p/Sed5p binding might be relevant for cargo selection during transport-vesicle formation and/or for vesicle targeting to the cis-Golgi. ..
  14. Banfield D, Lewis M, Pelham H. A SNARE-like protein required for traffic through the Golgi complex. Nature. 1995;375:806-9 pubmed
    ..Our results indicate that a single t-SNARE can control more than one transport step, and provide the first candidate for a SNARE involved in intra-Golgi traffic. ..
  15. Peng R, De Antoni A, Gallwitz D. Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members. J Biol Chem. 2000;275:11521-8 pubmed
    ..The data presented strongly suggest that the Sec24p-related proteins function as COPII components. ..
  16. Peng R, Gallwitz D. Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes. J Cell Biol. 2002;157:645-55 pubmed
    ..This indicates for the first time that a Sec1 family member contributes to the specificity of SNARE complex assembly. ..
  17. Flanagan J, Mukherjee I, Barlowe C. Examination of Sec22 Homodimer Formation and Role in SNARE-dependent Membrane Fusion. J Biol Chem. 2015;290:10657-66 pubmed publisher
    ..Sec22 is also reported to function in macroautophagy and in formation of endoplasmic reticulum-plasma membrane contact sites therefore homodimer assembly may regulate Sec22 activity across a range of cellular processes. ..
  18. Cho J, Noda Y, Yoda K. Proteins in the early golgi compartment of Saccharomyces cerevisiae immunoisolated by Sed5p. FEBS Lett. 2000;469:151-4 pubmed
    ..To better understand this compartment, we immunoisolated a membrane subfraction having Sed5p on the surface (the Sed5 vesicles)...
  19. Conchon S, Cao X, Barlowe C, Pelham H. Got1p and Sft2p: membrane proteins involved in traffic to the Golgi complex. EMBO J. 1999;18:3934-46 pubmed
    ..Sft2p is a non-essential tetra-spanning membrane protein, found mostly in the late Golgi, that can suppress some sed5 alleles...
  20. Schindler C, Spang A. Interaction of SNAREs with ArfGAPs precedes recruitment of Sec18p/NSF. Mol Biol Cell. 2007;18:2852-63 pubmed
  21. Dilcher M, Veith B, Chidambaram S, Hartmann E, Schmitt H, Fischer von Mollard G. Use1p is a yeast SNARE protein required for retrograde traffic to the ER. EMBO J. 2003;22:3664-74 pubmed
    ..Therefore, we conclude that Use1p is a novel SNARE protein that functions in retrograde traffic from the Golgi to the ER. ..
  22. Liu Y, Flanagan J, Barlowe C. Sec22p export from the endoplasmic reticulum is independent of SNARE pairing. J Biol Chem. 2004;279:27225-32 pubmed
    ..We propose that the COPII budding machinery has a preference for unassembled ER/Golgi SNARE proteins. ..
  23. Leznicki P, Clancy A, Schwappach B, High S. Bat3 promotes the membrane integration of tail-anchored proteins. J Cell Sci. 2010;123:2170-8 pubmed publisher
  24. Luo Z, Gallwitz D. Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments. J Biol Chem. 2003;278:791-9 pubmed
    ..The results obtained indicate that Ypt6p acts in endosome-to-Golgi, in intra-Golgi retrograde transport, and possibly also in Golgi-to-ER trafficking. ..
  25. Furukawa N, Mima J. Multiple and distinct strategies of yeast SNAREs to confer the specificity of membrane fusion. Sci Rep. 2014;4:4277 pubmed publisher
    ..Thus, our findings uncover multiple and distinct strategies of SNAREs to directly mediate fusion specificity. ..
  26. Kama R, Kanneganti V, Ungermann C, Gerst J. The yeast Batten disease orthologue Btn1 controls endosome-Golgi retrograde transport via SNARE assembly. J Cell Biol. 2011;195:203-15 pubmed publisher
    ..Specifically, BTN1 overexpression and deletion have opposing effects on phosphorylation of the Sed5 target membrane SNARE, on Golgi SNARE assembly, and on Golgi integrity...
  27. Shestakova A, Suvorova E, Pavliv O, Khaidakova G, Lupashin V. Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability. J Cell Biol. 2007;179:1179-92 pubmed
    ..These data suggest that the COG complex orchestrates vesicular trafficking similarly in yeast and mammalian cells by binding to the t-SNARE Syntaxin5a/Sed5p and enhancing the stability of intra-Golgi SNARE complexes. ..
  28. Zou S, Sun D, Liang Y. The Roles of the SNARE Protein Sed5 in Autophagy in Saccharomyces cerevisiae. Mol Cells. 2017;40:643-654 pubmed publisher
    ..In yeast, the cis-Golgi localized t-SNARE protein Sed5 plays a role in endoplasmic reticulum (ER)-Golgi and intra-Golgi vesicular transport...
  29. Kosodo Y, Noda Y, Adachi H, Yoda K. Cooperation of Sly1/SM-family protein and sec18/NSF of Saccharomyces cerevisiae in disassembly of cis-SNARE membrane-protein complexes. Biosci Biotechnol Biochem. 2003;67:448-50 pubmed
    ..The SM-family Slyl protein binds to the tSNARE Sed5 protein and stimulates its assembly into a trans-SNARE complex...
  30. Miller E, Liu Y, Barlowe C, Schekman R. ER-Golgi transport defects are associated with mutations in the Sed5p-binding domain of the COPII coat subunit, Sec24p. Mol Biol Cell. 2005;16:3719-26 pubmed
    ..We propose that the A-site of Sec24p is a multipurpose cargo-binding site that must recognize additional unidentified cargo proteins, at least one of which is essential at a late stage of vesicle fusion...
  31. Schuldiner M, Metz J, Schmid V, Denic V, Rakwalska M, Schmitt H, et al. The GET complex mediates insertion of tail-anchored proteins into the ER membrane. Cell. 2008;134:634-45 pubmed publisher
    ..Thus, the GET complex represents a critical mechanism for ensuring efficient and accurate targeting of TA proteins. ..
  32. Braun S, Jentsch S. SM-protein-controlled ER-associated degradation discriminates between different SNAREs. EMBO Rep. 2007;8:1176-82 pubmed
    ..This mechanism is specific for Ufe1, as the stability of another Sly1 partner, the Golgi Qa-SNARE Sed5, is not influenced by Sly1 interaction...
  33. Schindler C, Rodriguez F, Poon P, Singer R, Johnston G, Spang A. The GAP domain and the SNARE, coatomer and cargo interaction region of the ArfGAP2/3 Glo3 are sufficient for Glo3 function. Traffic. 2009;10:1362-75 pubmed publisher
    ..Our data suggest that membrane-interaction modules and cargo-sensing regions have evolved independently in ArfGAP1s versus ArfGAP2/3s. ..
  34. Kamena F, Diefenbacher M, Kilchert C, Schwarz H, Spang A. Ypt1p is essential for retrograde Golgi-ER transport and for Golgi maintenance in S. cerevisiae. J Cell Sci. 2008;121:1293-302 pubmed publisher
    ..Finally, COPI vesicles generated from Deltaypt1/SLY1-20 Golgi membranes in vitro were depleted of Emp47p and Sec22p. These data demonstrate that Ypt1p plays an essential role in retrograde transport from the Golgi to the ER. ..
  35. Lewis M, Rayner J, Pelham H. A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum. EMBO J. 1997;16:3017-24 pubmed
  36. Kosodo Y, Noda Y, Adachi H, Yoda K. Binding of Sly1 to Sed5 enhances formation of the yeast early Golgi SNARE complex. J Cell Sci. 2002;115:3683-91 pubmed
    ..The amount of Sly1 protein that coprecipitated with the t-SNARE Sed5 was much reduced in a temperature-sensitive sly1(ts) mutant yeast compared with the wildtype...
  37. Li Y, Gallwitz D, Peng R. Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum. Mol Biol Cell. 2005;16:3951-62 pubmed
    ..Together, these results indicate a previously unrecognized function of Sly1p in retrograde transport to the endoplasmic reticulum. ..
  38. Dulubova I, Yamaguchi T, Gao Y, Min S, Huryeva I, Sudhof T, et al. How Tlg2p/syntaxin 16 'snares' Vps45. EMBO J. 2002;21:3620-31 pubmed
    ..Thus, this mechanism represents the most widespread mode of coupling between syntaxins and SM proteins. ..
  39. Cao X, Ballew N, Barlowe C. Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J. 1998;17:2156-65 pubmed
    ..We propose that an initial vesicle docking event of ER-derived vesicles, termed tethering, depends on Uso1p and Ypt1p but is independent of SNARE proteins...
  40. Sacher M, Jiang Y, Barrowman J, Scarpa A, Burston J, Zhang L, et al. TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion. EMBO J. 1998;17:2494-503 pubmed
    ..TRAPP contains at least nine other constituents, five of which have been identified and shown to be highly conserved novel proteins. ..
  41. Peng R, Gallwitz D. Multiple SNARE interactions of an SM protein: Sed5p/Sly1p binding is dispensable for transport. EMBO J. 2004;23:3939-49 pubmed
    ..The newly identified, direct interactions of the SM protein with nonsytaxin SNAREs might provide a molecular mechanism by which SNAREs can be activated to engage in pairing and assemble into fusogenic SNARE complexes. ..
  42. Mossessova E, Bickford L, Goldberg J. SNARE selectivity of the COPII coat. Cell. 2003;114:483-95 pubmed
    ..Here, we show that recognition of the ER-Golgi SNAREs Bet1, Sed5, and Sec22 occurs through three binding sites on the Sec23/24 subcomplex of yeast COPII...
  43. Todorow Z, Spang A, Carmack E, Yates J, Schekman R. Active recycling of yeast Golgi mannosyltransferase complexes through the endoplasmic reticulum. Proc Natl Acad Sci U S A. 2000;97:13643-8 pubmed
    ..These observations indicate that the Mnn9p-containing mannosyltransferase complexes cycle back and forth between the ER and Golgi. ..
  44. Graf C, Riedel D, Schmitt H, Jahn R. Identification of functionally interacting SNAREs by using complementary substitutions in the conserved '0' layer. Mol Biol Cell. 2005;16:2263-74 pubmed
    ..The sec22(Q)/sed5(R) mutant is temperature sensitive and is rescued by a compensating R-->Q replacement in the R-SNARE Ykt6p...
  45. Meiringer C, Rethmeier R, Auffarth K, Wilson J, Perz A, Barlowe C, et al. The Dsl1 protein tethering complex is a resident endoplasmic reticulum complex, which interacts with five soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptors (SNAREs): implications for fusion and fusion regulation. J Biol Chem. 2011;286:25039-46 pubmed publisher
    ..Our data support a model, in which a tethering complex is stabilized at the organelle membrane by binding to SNAREs, recognizes the incoming vesicle via its coat and then promotes its SNARE-mediated fusion. ..
  46. Gourlay C, Dewar H, Warren D, Costa R, Satish N, Ayscough K. An interaction between Sla1p and Sla2p plays a role in regulating actin dynamics and endocytosis in budding yeast. J Cell Sci. 2003;116:2551-64 pubmed
    ..We propose that Sla2p recruits Sla1p to endocytic sites. Sla1p and its associated protein Pan1p then regulate actin assembly through interactions with Arp2/3 and Arp2/3-activating proteins Abp1p and Las17/Bee1p. ..
  47. Miller E, Antonny B, Hamamoto S, Schekman R. Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J. 2002;21:6105-13 pubmed
    ..Our data suggest that the principle role of Sec24p is to discriminate cargo molecules for incorporation into COPII vesicles...