SEC24/YIL109C Literature Guide Help

Other names published for SEC24: ANU1, YIL109C

SEC24 - Strains/Constructs (25)

ReferenceOther Genes Addressed
Copic A, et al.  (2012) ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p. Science 335(6074):1359-62
Okamoto M, et al.  (2012) High-curvature domains of the ER are important for the organization of ER exit sites in Saccharomyces cerevisiae. J Cell Sci 125(Pt 14):3412-20
Kodera C, et al.  (2011) Sed4p stimulates sar1p GTP hydrolysis and promotes limited coat disassembly. Traffic 12(5):591-9
Buchanan R, et al.  (2010) Genetic Analysis of Yeast Sec24p Mutants Suggests Cargo Binding Is Not Co-operative during ER Export. Traffic 11(8):1034-43
Levi SK, et al.  (2010) The Yeast GRASP Grh1 Colocalizes with COPII and Is Dispensable for Organizing the Secretory Pathway. Traffic 11(9):1168-79
Shindiapina P and Barlowe C  (2010) Requirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiae. Mol Biol Cell 21(9):1530-45
Tabata KV, et al.  (2009) Visualization of cargo concentration by COPII minimal machinery in a planar lipid membrane. EMBO J 28(21):3279-89
Cai H, et al.  (2007) TRAPPI tethers COPII vesicles by binding the coat subunit Sec23. Nature 445(7130):941-4
Pagant S, et al.  (2007) 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 18(9):3398-413
Karhinen L, et al.  (2005) Endoplasmic reticulum exit of a secretory glycoprotein in the absence of sec24p family proteins in yeast. Traffic 6(7):562-74
Lee MC, et al.  (2005) Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 122(4):605-17
Miller EA, et al.  (2005) ER-Golgi transport defects are associated with mutations in the Sed5p-binding domain of the COPII coat subunit, Sec24p. Mol Biol Cell 16(8):3719-26
Sato K and Nakano A  (2005) Reconstitution of cargo-dependent COPII coat assembly on proteoliposomes. Methods Enzymol 404():83-94
Fatal N, et al.  (2004) Active and specific recruitment of a soluble cargo protein for endoplasmic reticulum exit in the absence of functional COPII component Sec24p. J Cell Sci 117(Pt 9):1665-73
Hamasaki M, et al.  (2003) The early secretory pathway contributes to autophagy in yeast. Cell Struct Funct 28(1):49-54
Higashio H and Kohno K  (2002) A genetic link between the unfolded protein response and vesicle formation from the endoplasmic reticulum. Biochem Biophys Res Commun 296(3):568-74
Ishihara N, et al.  (2001) Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Mol Biol Cell 12(11):3690-702
Kim DW, et al.  (2001) Sgf1p, a new component of the Sec34p/Sec35p complex. Traffic 2(11):820-30
De Antoni A and Gallwitz D  (2000) A novel multi-purpose cassette for repeated integrative epitope tagging of genes in Saccharomyces cerevisiae. Gene 246(1-2):179-85
Higashio H, et al.  (2000) 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 275(23):17900-8
Kurihara T, et al.  (2000) Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae. Mol Biol Cell 11(3):983-98
Shimoni Y, et al.  (2000) Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J Cell Biol 151(5):973-84
Penalver E, et al.  (1999) Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter. J Bacteriol 181(8):2555-63
Peng R, et al.  (1999) 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 96(7):3751-6
Roberg KJ, et al.  (1999) LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. J Cell Biol 145(4):659-72