Gene Symbol: SEC24
Description: COPII subunit SEC24
Alias: ANU1, COPII subunit SEC24
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Shaywitz D, Espenshade P, Gimeno R, Kaiser C. COPII subunit interactions in the assembly of the vesicle coat. J Biol Chem. 1997;272:25413-6 pubmed
    ..We propose that Sec16p organizes the assembly of a coat that is stabilized both by the interaction of Sec31p with Sec23p and Sec24p and by the interaction of these three components with Sec16p...
  2. Springer S, Schekman R. Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs. Science. 1998;281:698-700 pubmed
    ..The data suggest that transmembrane proteins can be taken up into COPII vesicles by direct interactions with the coat proteins and may play a structural role in the assembly of the COPII coat complex...
  3. Roberg K, Crotwell M, Espenshade P, Gimeno R, Kaiser C. LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. J Cell Biol. 1999;145:659-72 pubmed
    ..Together, these findings suggest that a specialized form of the COPII coat subunit, with Lst1p in place of Sec24p, is used for the efficient packaging of Pma1p into vesicles derived from the ER. ..
  4. Matsuoka K, Schekman R. The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting. Methods. 2000;20:417-28 pubmed
    ..Therefore, both generation of coated vesicles and protein sorting into the vesicles can be reproduced with liposomes and purified proteins. ..
  5. Mossessova E, Bickford L, Goldberg J. SNARE selectivity of the COPII coat. Cell. 2003;114:483-95 pubmed
    ..The COPII coat seems to be a specific conductor of the fusogenic forms of these SNAREs, suggesting how vesicle fusion specificity may be programmed during budding...
  6. Barlowe C, Orci L, Yeung T, Hosobuchi M, Hamamoto S, Salama N, et al. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell. 1994;77:895-907 pubmed
    ..Because the overall cycle of budding driven by these two types of coats appears mechanistically similar, we propose that the coat structures be called COPI and COPII. ..
  7. Gimeno R, Espenshade P, Kaiser C. COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p. Mol Biol Cell. 1996;7:1815-23 pubmed
    ..These findings define binding to Sec16p as a new function for Sec24p and support the idea that Sec16p organizes assembly of the COPII coat...
  8. 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...
  9. Kung L, Pagant S, Futai E, D Arcangelo J, Buchanan R, Dittmar J, et al. Sec24p and Sec16p cooperate to regulate the GTP cycle of the COPII coat. EMBO J. 2012;31:1014-27 pubmed publisher
    ..We have identified a novel mutation (sec24-m11) in the cargo-binding subunit, Sec24p, that specifically impacts the GTP-dependent generation of vesicles in ..

More Information


  1. Lord C, Bhandari D, Menon S, Ghassemian M, Nycz D, HAY J, et al. Sequential interactions with Sec23 control the direction of vesicle traffic. Nature. 2011;473:181-6 pubmed publisher
    ..These events are conserved in mammalian cells. ..
  2. Kurihara T, Hamamoto S, Gimeno R, Kaiser C, Schekman R, Yoshihisa T. Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae. Mol Biol Cell. 2000;11:983-98 pubmed
    ..Here we characterize Saccharomyces cerevisiae SEC24, which encodes a protein of 926 amino acids (YIL109C), and a close homologue, ISS1 (YNL049C), which is 55% ..
  3. 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. ..
  4. 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
    ..We generated several conditional-lethal sec24 mutants that, combined with null alleles of SFB2 and SFB3/LST1, led to a complete block of transport between the ..
  5. Supek F, Madden D, Hamamoto S, Orci L, Schekman R. Sec16p potentiates the action of COPII proteins to bud transport vesicles. J Cell Biol. 2002;158:1029-38 pubmed
    ..We propose that Sec16p nucleates a Sar1-GTP-dependent initiation of COPII assembly and serves to stabilize the coat to premature disassembly after Sar1p hydrolyzes GTP...
  6. Bi X, Corpina R, Goldberg J. Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature. 2002;419:271-7 pubmed
    ..These observations establish the structural basis for GTP-dependent recruitment of a vesicular coat complex, and for uncoating through coat-controlled GTP hydrolysis...
  7. Shimoni Y, Kurihara T, Ravazzola M, Amherdt M, Orci L, Schekman R. Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J Cell Biol. 2000;151:973-84 pubmed
    ..By changing the geometry of COPII coat polymerization, Lst1p may allow the transport of bulky cargo molecules, polymers, or particles...
  8. Votsmeier C, Gallwitz D. An acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export. EMBO J. 2001;20:6742-50 pubmed
    ..Our study demonstrates for the first time that, in yeast, a di-acidic sequence motif can act as a sorting signal for cargo selection during the formation of transport vesicles at the ER by direct binding to COPII component(s). ..
  9. Pagant S, Kung L, DORRINGTON M, Lee M, Miller E. Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal. Mol Biol Cell. 2007;18:3398-413 pubmed
    ..We propose that the ER quality control checkpoint engages misfolded Yor1p even after it has been stabilized by inhibition of the degradative pathway...
  10. Ishihara N, Hamasaki M, Yokota S, Suzuki K, Kamada Y, Kihara A, et al. Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Mol Biol Cell. 2001;12:3690-702 pubmed
    ..Three other coatmer protein (COPII) mutants, sec16, sec23, and sec24, were also defective in autophagy...
  11. Davis S, Wang J, Zhu M, Stahmer K, Lakshminarayan R, Ghassemian M, et al. Sec24 phosphorylation regulates autophagosome abundance during nutrient deprivation. elife. 2016;5: pubmed publisher
    ..conserved amino acids on the membrane-distal surface of the Saccharomyces cerevisiae COPII cargo adaptor, Sec24, reprograms COPII vesicles for autophagy...
  12. Iwasaki H, Yorimitsu T, Sato K. Distribution of Sec24 isoforms to each ER exit site is dynamically regulated in Saccharomyces cerevisiae. FEBS Lett. 2015;589:1234-9 pubmed publisher
    ..These results suggest that in S. cerevisiae cargo loading to ERES is dynamically controlled in response to environmental changes. ..
  13. Copic A, Latham C, Horlbeck M, D Arcangelo J, Miller E. ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p. Science. 2012;335:1359-62 pubmed publisher
    ..Thus, Sec13p may rigidify the COPII cage and increase its membrane-bending capacity; this function could be bypassed when a bst mutation renders the membrane more deformable. ..
  14. Sato K, Nakano A. Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting. J Biol Chem. 2004;279:1330-5 pubmed
    ..Furthermore, this GTP hydrolysis decreases the error of cargo sorting. We suggest that GTP hydrolysis by Sar1p promotes exclusion of improper proteins from COPII vesicles. ..
  15. Cohen M, Stutz F, Belgareh N, Haguenauer Tsapis R, Dargemont C. Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. Nat Cell Biol. 2003;5:661-7 pubmed
    ..This probably contributes to maintaining and adapting a Sec23 expression level that is compatible with an efficient secretion pathway, and consequently with cell growth and viability. ..
  16. Lederkremer G, Cheng Y, Petre B, Vogan E, Springer S, Schekman R, et al. Structure of the Sec23p/24p and Sec13p/31p complexes of COPII. Proc Natl Acad Sci U S A. 2001;98:10704-9 pubmed
    ..Putting together the architecture of these Sec complexes with the interactions between their subunits and the appearance of the coat in COPII-coated vesicles, we present a model for COPII coat organization...
  17. Higashio H, Kohno K. A genetic link between the unfolded protein response and vesicle formation from the endoplasmic reticulum. Biochem Biophys Res Commun. 2002;296:568-74 pubmed
    ..participate in the formation of COPII-coated vesicles (COPII vesicles), we isolated high-copy suppressors of a sec24-20 mutant defective in COPII vesicle formation from the ER at the restrictive temperature...
  18. Antonny B, Gounon P, Schekman R, Orci L. Self-assembly of minimal COPII cages. EMBO Rep. 2003;4:419-24 pubmed
    ..We suggest that these structures, which represent a minimal COPII cage, mimic the molecular organization of the membrane-associated COPII coat...
  19. Yorimitsu T, Sato K. Insights into structural and regulatory roles of Sec16 in COPII vesicle formation at ER exit sites. Mol Biol Cell. 2012;23:2930-42 pubmed publisher
    ..These features ensure prolonged COPII coat association within a preformed Sec16 cluster, which may lead to the formation of ERES. Our results indicate a mechanistic relationship between COPII coat assembly and ERES formation. ..
  20. Gilstring C, Melin Larsson M, Ljungdahl P. Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles. Mol Biol Cell. 1999;10:3549-65 pubmed
  21. 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
    ..Our findings suggest that co-operativity does not influence cargo capture at these sites, and that Sec22p rescue occurs via its function as a retrograde SNARE. ..
  22. Rein U, Andag U, Duden R, Schmitt H, Spang A. ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat. J Cell Biol. 2002;157:395-404 pubmed
    ..The mechanisms by which v-SNAREs interact with COPI and COPII coat proteins seem to be different and may play a key role in determining specificity in vesicle budding...
  23. Fatal N, Karhinen L, Jokitalo E, Makarow M. Active and specific recruitment of a soluble cargo protein for endoplasmic reticulum exit in the absence of functional COPII component Sec24p. J Cell Sci. 2004;117:1665-73 pubmed
    ..Here we show that its ER exit did not require functional Sec24p. Hsp150 was secreted to the medium in a sec24-1 mutant at restrictive temperature 37 degrees C, while cell wall invertase and vacuolar carboxypeptidase Y ..
  24. Miller E, Beilharz T, Malkus P, Lee M, Hamamoto S, Orci L, et al. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell. 2003;114:497-509 pubmed
    ..Together, our data support a model whereby Sec24p proteins contain multiple independent cargo binding domains that allow for recognition of a diverse set of sorting signals...
  25. Deitz S, Rambourg A, Kepes F, Franzusoff A. Sec7p directs the transitions required for yeast Golgi biogenesis. Traffic. 2000;1:172-83 pubmed
  26. Barlowe C. Three-dimensional structure of a COPII prebudding complex. Dev Cell. 2002;3:467-8 pubmed
    ..Crystallographic analysis of a Sec23/24-Sar1 prebudding complex of COPII now provides a molecular view of this GTPase-directed coat assembly mechanism. ..
  27. Higashio H, Kimata Y, Kiriyama T, Hirata A, Kohno K. Sfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum. J Biol Chem. 2000;275:17900-8 pubmed
    ..Based on the finding that ANU1 is identical to SEC24, we confirmed a temperature-sensitive protein transport from the ER to the Golgi in anu1-1/sec24-20 cells...
  28. 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...
  29. Behnia R, Barr F, Flanagan J, Barlowe C, Munro S. The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic. J Cell Biol. 2007;176:255-61 pubmed
  30. Sandmann T, Herrmann J, Dengjel J, Schwarz H, Spang A. Suppression of coatomer mutants by a new protein family with COPI and COPII binding motifs in Saccharomyces cerevisiae. Mol Biol Cell. 2003;14:3097-113 pubmed
    ..As a consequence, the amount of cargo that can bind COPI might be important for the regulation of the vesicle flow in the early secretory pathway. ..
  31. Powers J, Barlowe C. Erv14p directs a transmembrane secretory protein into COPII-coated transport vesicles. Mol Biol Cell. 2002;13:880-91 pubmed
    ..Based on these results and further genetic experiments, we propose Erv14p coordinates COPII vesicle formation with incorporation of specific secretory cargo. ..
  32. Jakobsen M, Cheng Z, Lam S, Roth Johnson E, Barfield R, Schekman R. Phosphorylation of Chs2p regulates interaction with COPII. J Cell Sci. 2013;126:2151-6 pubmed publisher
    ..Our data suggest that dephosphorylation functions as a molecular switch for regulated ER exit of Chs2p. ..
  33. Bhandari D, Zhang J, Menon S, Lord C, Chen S, Helm J, et al. Sit4p/PP6 regulates ER-to-Golgi traffic by controlling the dephosphorylation of COPII coat subunits. Mol Biol Cell. 2013;24:2727-38 pubmed publisher
    ..In vitro, Sit4p dephosphorylates COPII coat subunits. Consistent with a role in coat recycling, Sit4p and its mammalian orthologue, PP6, regulate traffic from the ER to the Golgi complex. ..
  34. Kodera C, Yorimitsu T, Sato K. Sec23 homolog Nel1 is a novel GTPase-activating protein for Sar1 but does not function as a subunit of the coat protein complex II (COPII) coat. J Biol Chem. 2014;289:21423-32 pubmed publisher
    ..In contrast to Sec23, which is predominantly localized at ER exit sites on the ER membrane, a major proportion of Nel1 is localized throughout the cytosol. Our findings highlight a possible role of Nel1 as a novel GAP for Sar1. ..
  35. Kim D, Massey T, Sacher M, Pypaert M, Ferro Novick S. Sgf1p, a new component of the Sec34p/Sec35p complex. Traffic. 2001;2:820-30 pubmed
    ..Although an earlier study suggested that Sec34p (Grd20p) is not required for protein secretion, we show here that the sec34-2 and sec35-1 mutations lead to a pleiotropic block in the secretion of all proteins into the growth medium. ..
  36. Belden W, Barlowe C. Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex. J Biol Chem. 2001;276:43040-8 pubmed
    ..The Erv25p tail sequence binds COPI and is responsible for returning this complex to the ER. ..
  37. 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. ..
  38. Pagant S, Wu A, EDWARDS S, Diehl F, Miller E. Sec24 is a coincidence detector that simultaneously binds two signals to drive ER export. Curr Biol. 2015;25:403-12 pubmed publisher
    ..secretory proteins into ER-derived vesicles involves recognition of cytosolic signals by the COPII coat protein, Sec24. Additional cargo diversity is achieved through cargo receptors, which include the Erv14/Cornichon family that ..