Genomes and Genes
Gene Symbol: SEC22
Description: SNAP receptor SEC22
Alias: SLY2, TS26, TSL26, SNAP receptor SEC22
Species: Saccharomyces cerevisiae S288c
- Poon P, Cassel D, Spang A, Rotman M, Pick E, Singer R, et al. Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function. EMBO J. 1999;18:555-64 pubmed..COPI, which mediates vesicular transport within the ER-Golgi shuttle, while increased dosage of the BET1, BOS1 and SEC22 genes encoding members of a v-SNARE family that functions within the ER-Golgi alleviates the effects of a ..
- Kim D, Sacher M, Scarpa A, Quinn A, Ferro Novick S. High-copy suppressor analysis reveals a physical interaction between Sec34p and Sec35p, a protein implicated in vesicle docking. Mol Biol Cell. 1999;10:3317-29 pubmed..Sec34p and Sec35p stably associate with each other to form a multiprotein complex of approximately 480 kDa. These data indicate that Sec34p acts in conjunction with Sec35p to mediate a common step in vesicular traffic. ..
- Newman A, Shim J, Ferro Novick S. BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex. Mol Cell Biol. 1990;10:3405-14 pubmed..genetic interactions among these genes and another gene implicated in transport from the ER to the Golgi complex: SEC22. Overproduction of either BET1 or BOS1 suppresses the growth and secretory defects of the sec22-3 mutant over a ..
- 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. ..
- 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
- Duden R, Hosobuchi M, Hamamoto S, Winey M, Byers B, Schekman R. Yeast beta- and beta'-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic. J Biol Chem. 1994;269:24486-95 pubmed..Genetic interactions connect sec27-1 and sec21-1 (coatomer gamma subunit) with the ARF1 and ARF2 genes and with the SEC22, BET1, and BOS1 genes, which encode membrane proteins involved in ER-to-Golgi transport.
- Rexach M, Latterich M, Schekman R. Characteristics of endoplasmic reticulum-derived transport vesicles. J Cell Biol. 1994;126:1133-48 pubmed..in vitro incubations, carry lumenal and membrane proteins that include core-glycosylated pro-alpha-factor, Bet1, Sec22, and Bos1, but not ER-resident Kar2 or Sec61 proteins...
- Spang A, Schekman R. Reconstitution of retrograde transport from the Golgi to the ER in vitro. J Cell Biol. 1998;143:589-99 pubmed..Putative retrograde carriers (COPI vesicles) generated from Golgi-enriched membranes contain v-SNAREs as well as Emp47p as cargo...
- Jiang Y, Scarpa A, Zhang L, Stone S, Feliciano E, Ferro Novick S. A high copy suppressor screen reveals genetic interactions between BET3 and a new gene. Evidence for a novel complex in ER-to-Golgi transport. Genetics. 1998;149:833-41 pubmed..of the bet5-1 mutant include several genes whose products are required for ER-to-Golgi transport (BET1, SEC22, USO1 and DSS4) and the maintenance of the Golgi (ANP1)...
- 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..Sed5 is known to combine with two light chains (Bos1 and Sec22) to form the t-SNARE needed to receive vesicles from the endoplasmic reticulum...
- VanRheenen S, Cao X, Sapperstein S, Chiang E, Lupashin V, Barlowe C, et al. Sec34p, a protein required for vesicle tethering to the yeast Golgi apparatus, is in a complex with Sec35p. J Cell Biol. 1999;147:729-42 pubmed..Finally, we describe RUD3, a novel gene identified through a genetic screen for multicopy suppressors of a mutation in USO1, which suppresses the sec34-2 mutation as well. ..
- Andag U, Neumann T, Schmitt H. The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast. J Biol Chem. 2001;276:39150-60 pubmed..We isolated mutant yeast strains in which SEC22 gene function, which in a wild type strain background is non-essential for cell viability, has become essential...
- Liu Y, Barlowe C. Analysis of Sec22p in endoplasmic reticulum/Golgi transport reveals cellular redundancy in SNARE protein function. Mol Biol Cell. 2002;13:3314-24 pubmed
- 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
- Sapperstein S, Lupashin V, Schmitt H, Waters M. Assembly of the ER to Golgi SNARE complex requires Uso1p. J Cell Biol. 1996;132:755-67 pubmed..Finally, biochemical analysis indicates that Uso1p, like Ypt1p, is required for assembly of the v-SNARE/t-SNARE complex. The implications of these findings, with respect to the mechanism of vesicle docking, are discussed. ..
- Rossi G, Kolstad K, Stone S, Palluault F, Ferro Novick S. BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs. Mol Biol Cell. 1995;6:1769-80 pubmed..These findings support the hypothesis that Bet3p may act before the assembly of the SNARE complex. ..
- 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. ..
- 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..Sec22p, a v-SNARE implicated in forward transport from ER to Golgi, co-precipitates with Ufe1p and Sec20p, and SEC22 acts as an allele-specific multicopy suppressor of a temperature-sensitive ufe1 mutation...
- Burri L, Varlamov O, Doege C, Hofmann K, Beilharz T, Rothman J, et al. A SNARE required for retrograde transport to the endoplasmic reticulum. Proc Natl Acad Sci U S A. 2003;100:9873-7 pubmed..Slt1 is an essential protein localized in the endoplasmic reticulum (ER). It forms a SNARE complex with Sec22 and the ER syntaxin Ufe1...
- 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. ..
- 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. ..
- Ballensiefen W, Ossipov D, Schmitt H. Recycling of the yeast v-SNARE Sec22p involves COPI-proteins and the ER transmembrane proteins Ufe1p and Sec20p. J Cell Sci. 1998;111 ( Pt 11):1507-20 pubmed..The v-SNARE Sec22(Sly2)p mediates the targeting of vesicles between endoplasmic reticulum (ER) and early Golgi of Saccharomyces ..
- Ossig R, Dascher C, Trepte H, Schmitt H, Gallwitz D. The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport. Mol Cell Biol. 1991;11:2980-93 pubmed..These suppressors also partially complement the sec21-1 and sec22-3 mutants which lead to a defect early in the secretory pathway...
- 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 for ..
- VanRheenen S, Cao X, Lupashin V, Barlowe C, Waters M. Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking. J Cell Biol. 1998;141:1107-19 pubmed..Weaker suppression is evident upon overexpression of genes encoding the vesicle-SNAREs SEC22, BET1, or YKT6. The cold-sensitive lethality that results from deleting SEC35 is suppressed by YPT1 or SLY1-20...
- Kito M, Seog D, Igarashi K, Kambe Honjo H, Yoda K, Yamasaki M. Calcium and SLY genes suppress the temperature-sensitive secretion defect of Saccharomyces cerevisiae uso1 mutant. Biochem Biophys Res Commun. 1996;220:653-7 pubmed..The common phenotype and suppression of the mutants suggest that Uso1 and Ypt1 proteins function in the same process of protein transport, i.e., targeting or fusion of the transport vesicles to the Golgi membrane. ..
- Diefenbacher M, Thorsteinsdóttir H, Spang A. The Dsl1 tethering complex actively participates in soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (SNARE) complex assembly at the endoplasmic reticulum in Saccharomyces cerevisiae. J Biol Chem. 2011;286:25027-38 pubmed publisher..We provide evidence for a direct role of the Dsl1 complex, in particular Tip20p, in the formation and stabilization of ER SNARE complexes. ..
- Lian J, Ferro Novick S. Bos1p, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence. Cell. 1993;73:735-45 pubmed..integral endoplasmic reticulum (ER) membrane protein and genetically interacts with three other yeast genes (BET1, SEC22, and YPT1) whose products are required for membrane traffic between the ER and the Golgi apparatus...
- 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. ..
- 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...
- Friesen H, Colwill K, Robertson K, Schub O, Andrews B. Interaction of the Saccharomyces cerevisiae cortical actin patch protein Rvs167p with proteins involved in ER to Golgi vesicle trafficking. Genetics. 2005;170:555-68 pubmed..Since Rvs167p has a previously characterized role in endocytosis and we have shown here that it interacts with proteins involved in Golgi vesicle trafficking, we suggest that Rvs167p may have a general role in vesicle trafficking. ..
- Nair U, Jotwani A, Geng J, Gammoh N, Richerson D, Yen W, et al. SNARE proteins are required for macroautophagy. Cell. 2011;146:290-302 pubmed publisher..Additionally, we found that the endosomal Q/t-SNARE Tlg2 and the R/v-SNAREs Sec22 and Ykt6 interact with Sso1-Sec9, and are required for normal Atg9 transport...
- Zhang Y, SchÃ¤ffer T, WÃ¶lfle T, Fitzke E, Thiel G, Rospert S. Cotranslational Intersection between the SRP and GET Targeting Pathways to the Endoplasmic Reticulum of Saccharomyces cerevisiae. Mol Cell Biol. 2016;36:2374-83 pubmed publisher..Ribosome binding of Get4-5 was independent of Sgt2 and was strongly outcompeted by SRP. The combined data indicate a previously unrecognized cotranslational interplay between the SRP and GET pathways. ..
- Kuehn M, Herrmann J, Schekman R. COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature. 1998;391:187-90 pubmed..Our results indicate that cargo packaging signals and soluble cargo adaptors are recognized by a recruitment complex comprising Sar1-GTP and Sec23/24...
- Lee M, Ko Y, Moon Y, Han M, Kim H, Lee S, et al. SNAREs support atlastin-mediated homotypic ER fusion in Saccharomyces cerevisiae. J Cell Biol. 2015;210:451-70 pubmed publisher..Collectively, our data strongly suggest that SNARE-mediated membrane fusion is involved in atlastin-initiated homotypic ER fusion. ..
- Qi C, Zhang H, Liu L, Yang R, Yang Y, Kang T, et al. Analysis of interactions between SNARE proteins using imaging ellipsometer coupled with microfluidic array. Sci Rep. 2014;4:5341 pubmed publisher..We argue that the use of imaging ellipsometer coupled with microfluidic device will deepen our understanding of the molecular mechanisms underlying membrane fusion process. ..
- 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. ..
- Rogers J, Arlow T, Inkellis E, Koo T, Rose M. ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating. Mol Biol Cell. 2013;24:3896-908 pubmed publisher..Together these data demonstrate that SNAREs mediate nuclear fusion, ER fusion after cell fusion is necessary to complete nuclear congression, and there exists a SNARE-mediated, Sey1p-independent ER fusion pathway. ..
- 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. ..
- Sato K, Nakano A. Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis. Nat Struct Mol Biol. 2005;12:167-74 pubmed..These data suggest a model for the maintenance of kinetically stable prebudding complexes during the Sar1p GTPase cycle that regulates cargo sorting into transport vesicles. ..
- Bacon R, Salminen A, Ruohola H, Novick P, Ferro Novick S. The GTP-binding protein Ypt1 is required for transport in vitro: the Golgi apparatus is defective in ypt1 mutants. J Cell Biol. 1989;109:1015-22 pubmed..We have also established genetic interactions between ypt1 and a subset of the other genes required for transport to and through the Golgi apparatus. ..
- Wang F, Whynot A, Tung M, Denic V. The mechanism of tail-anchored protein insertion into the ER membrane. Mol Cell. 2011;43:738-50 pubmed publisher..Lastly, we show that ATP enhances Get3 dissociation from the membrane, thus freeing Get1-Get2 for new rounds of substrate insertion. ..
- Tsui M, Banfield D. Yeast Golgi SNARE interactions are promiscuous. J Cell Sci. 2000;113 ( Pt 1):145-52 pubmed
- Wang F, Brown E, Mak G, Zhuang J, Denic V. A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol Cell. 2010;40:159-71 pubmed publisher..Thus, ER-bound TA proteins are sorted at the top of a TMD chaperone cascade that culminates with the formation of Get3-TA protein complexes, which are recruited to the ER membrane for insertion. ..
- Buchanan R, Kaufman A, Kung Tran L, Miller E. Genetic analysis of yeast Sec24p mutants suggests cargo binding is not co-operative during ER export. Traffic. 2010;11:1034-43 pubmed publisher..We identified SMY2 as a general suppressor that rescued multiple defects in Sec24p, and SEC22 as a specific suppressor of two adjacent cargo-binding sites, raising the possibility of allosteric regulation of ..
- Noda Y, Yoda K. Svp26 facilitates endoplasmic reticulum to golgi transport of a set of mannosyltransferases in Saccharomyces cerevisiae. J Biol Chem. 2010;285:15420-9 pubmed publisher..The domain switching between Svp26-dependent Mnn2 or Ktr3 and Svp26-independent Mnn1 suggests that the lumenal domain of mannosyltransferases, but not the cytoplasmic or transmembrane domain, is responsible for recognition by Svp26. ..
- 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. ..
- Legesse Miller A, Sagiv Y, Glozman R, Elazar Z. Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes. J Biol Chem. 2000;275:32966-73 pubmed..In vivo, AUT7 interacts genetically with endoplasmic reticulum to Golgi SNAREs, specifically with BET1 and SEC22. Aut7p interacts physically with the following two v-SNAREs: Bet1p, which is involved in endoplasmic reticulum to ..
- Yamagata A, Mimura H, Sato Y, Yamashita M, Yoshikawa A, Fukai S. Structural insight into the membrane insertion of tail-anchored proteins by Get3. Genes Cells. 2010;15:29-41 pubmed publisher..This interaction is independent of ATP and dimer formation. Finally, we propose a structural mechanism that links ATP hydrolysis with the TA-protein insertion mediated by the conserved DTAPTGH motif. ..
- 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...
- 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..Here we monitored interactions of the R-SNARE protein Sec22 through a cysteine scanning approach and detected efficient formation of cross-linked Sec22 homodimers in cellular ..
- Kim D. Characterization of Grp1p, a novel cis-Golgi matrix protein. Biochem Biophys Res Commun. 2003;303:370-8 pubmed..5h incubation at 38.5 degrees C. Together, these data suggest that Grp1p is a novel matrix protein that is involved in the structural organization of the cis-Golgi. ..
- Shen D, Yuan H, Hutagalung A, Verma A, Kümmel D, Wu X, et al. The synaptobrevin homologue Snc2p recruits the exocyst to secretory vesicles by binding to Sec6p. J Cell Biol. 2013;202:509-26 pubmed publisher..We propose that the exocyst is recruited to secretory vesicles by the combinatorial signals of Sec4-GTP and the Snc proteins. This could help to confer both specificity and directionality to vesicular traffic. ..
- 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 ..
- 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..Here, we analyze molecular interactions between five SNAREs of the ER (Ufe1, Use1, Sec20, Sec22, and Ykt6) and the Dsl1 complex in vitro and in vivo...
- Flanagan J, Barlowe C. Cysteine-disulfide cross-linking to monitor SNARE complex assembly during endoplasmic reticulum-Golgi transport. J Biol Chem. 2006;281:2281-8 pubmed..This data suggests that Ca(2+) is not directly required for membrane fusion between ER-derived vesicles and Golgi-acceptor membranes. ..
- Mancias J, Goldberg J. The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope. Mol Cell. 2007;26:403-14 pubmed publisher..The SNARE protein Sec22 contains a signal that binds the COPII subcomplex Sec23/24 and specifies its endoplasmic reticulum (ER) exit as an ..
- Schindler C, Spang A. Interaction of SNAREs with ArfGAPs precedes recruitment of Sec18p/NSF. Mol Biol Cell. 2007;18:2852-63 pubmed
- 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
- Neiman A, Katz L, Brennwald P. Identification of domains required for developmentally regulated SNARE function in Saccharomyces cerevisiae. Genetics. 2000;155:1643-55 pubmed..Deletion studies indicate that activation and inhibition are separable functions of the Spo20p N terminus. Our results reveal an additional layer of regulation of the SNARE complex, which is necessary only in sporulating cells. ..
- Petkovic M, Jemaiel A, Daste F, Specht C, Izeddin I, Vorkel D, et al. The SNARE Sec22b has a non-fusogenic function in plasma membrane expansion. Nat Cell Biol. 2014;16:434-44 pubmed publisher..In yeast, Sec22 interacts with lipid transfer proteins, and inhibition of Sec22 leads to defects in lipid metabolism at contact ..
- Friedmann E, Salzberg Y, Weinberger A, Shaltiel S, Gerst J. YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins. J Biol Chem. 2002;277:35274-81 pubmed..As Yos9 is not a component of the Emp24 complex, it may act as a novel escort factor for GPI-anchored proteins in ER-Golgi transport in yeast and possibly in mammals. ..