SEC62/YPL094C Literature Guide Help

Other names published for SEC62: LPG14, YPL094C

SEC62 - Protein-protein Interactions (24)

ReferenceOther Genes Addressed
Falcone D, et al.  (2011) Stability and function of the Sec61 translocation complex depends on the Sss1p tail-anchor sequence. Biochem J 436(2):291-303
Harada Y, et al.  (2011) Structural Studies and the Assembly of the Heptameric Post-translational Translocon Complex. J Biol Chem 286(4):2956-65
Pina FJ, et al.  (2011) Hph1 and hph2 are novel components of the sec63/sec62 posttranslational translocation complex that aid in vacuolar proton ATPase biogenesis. Eukaryot Cell 10(1):63-71
Scott DC and Schekman R  (2008) Role of Sec61p in the ER-associated degradation of short-lived transmembrane proteins. J Cell Biol 181(7):1095-105
Ng W, et al.  (2007) Characterization of the proteasome interaction with the Sec61 channel in the endoplasmic reticulum. J Cell Sci 120(Pt 4):682-91
Wang X and Johnsson N  (2005) Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of the endoplasmic reticulum protein translocation apparatus. J Cell Sci 118(Pt 4):723-32
Plath K, et al.  (2004) Interactions between Sec complex and prepro-alpha-factor during posttranslational protein transport into the endoplasmic reticulum. Mol Biol Cell 15(1):1-10
Willer M, et al.  (2003) Identification of novel protein-protein interactions at the cytosolic surface of the Sec63 complex in the yeast ER membrane. Yeast 20(2):133-48
Morrow MW and Brodsky JL  (2001) Yeast ribosomes bind to highly purified reconstituted Sec61p complex and to mammalian p180. Traffic 2(10):705-16
Young BP, et al.  (2001) Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo. EMBO J 20(1-2):262-71
Wittke S, et al.  (2000) Sec62p, a component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the Sec-complex. Mol Biol Cell 11(11):3859-71
Dunnwald M, et al.  (1999) Detection of transient in vivo interactions between substrate and transporter during protein translocation into the endoplasmic reticulum. Mol Biol Cell 10(2):329-44
Wittke S, et al.  (1999) Probing the molecular environment of membrane proteins in vivo. Mol Biol Cell 10(8):2519-30
Plath K, et al.  (1998) Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 94(6):795-807
Lyman SK and Schekman R  (1997) Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 88(1):85-96
Matlack KE, et al.  (1997) Protein transport by purified yeast Sec complex and Kar2p without membranes. Science 277(5328):938-41
Finke K, et al.  (1996) A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J 15(7):1482-94
Hanein D, et al.  (1996) Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation. Cell 87(4):721-32
Schlenstedt G, et al.  (1995) A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s. J Cell Biol 129(4):979-88
Kurihara T and Silver P  (1993) Suppression of a sec63 mutation identifies a novel component of the yeast endoplasmic reticulum translocation apparatus. Mol Biol Cell 4(9):919-30
Musch A, et al.  (1992) Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane. Cell 69(2):343-52
Sanders SL, et al.  (1992) Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell 69(2):353-65
Deshaies RJ, et al.  (1991) Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex. Nature 349(6312):806-8
Deshaies RJ and Schekman R  (1990) Structural and functional dissection of Sec62p, a membrane-bound component of the yeast endoplasmic reticulum protein import machinery. Mol Cell Biol 10(11):6024-35