SEC63/YOR254C Literature Guide Help

Other names published for SEC63: PTL1, YOR254C

SEC63 - Protein-protein Interactions (38)

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
Hu L, et al.  (2011) Predicting protein phenotypes based on protein-protein interaction network. PLoS One 6(3):e17668
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
Vembar SS, et al.  (2010) J domain co-chaperone specificity defines the role of BiP during protein translocation. J Biol Chem 285(29):22484-94
Wilson JD and Barlowe C  (2010) Yet1p and Yet3p, the yeast homologs of BAP29 and BAP31, interact with the endoplasmic reticulum translocation apparatus and are required for inositol prototrophy. J Biol Chem 285(24):18252-61
Gong Y, et al.  (2009) An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol Syst Biol 5:275
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
Jermy AJ, et al.  (2006) The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons. J Biol Chem 281(12):7899-906
Xia Y, et al.  (2006) Integrated prediction of the helical membrane protein interactome in yeast. J Mol Biol 357(1):339-49
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
Kabani M, et al.  (2003) Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP. Mol Biol Cell 14(8):3437-48
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
Chevalier M, et al.  (2000) Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1. J Biol Chem 275(26):19620-7
Kabani M, et al.  (2000) Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum. Mol Cell Biol 20(18):6923-34
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
Matlack KE, et al.  (1999) BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell 97(5):553-64
Misselwitz B, et al.  (1999) Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex. J Biol Chem 274(29):20110-5
Sato K, et al.  (1999) The Arabidopsis thaliana RER1 gene family: its potential role in the endoplasmic reticulum localization of membrane proteins. Plant Mol Biol 41(6):815-24
Wittke S, et al.  (1999) Probing the molecular environment of membrane proteins in vivo. Mol Biol Cell 10(8):2519-30
Brodsky JL, et al.  (1998) Mitochondrial Hsp70 cannot replace BiP in driving protein translocation into the yeast endoplasmic reticulum. FEBS Lett 435(2-3):183-6
McClellan AJ, et al.  (1998) Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER. Mol Biol Cell 9(12):3533-45
Misselwitz B, et al.  (1998) J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol Cell 2(5):593-603
Corsi AK and Schekman R  (1997) The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae. J Cell Biol 137(7):1483-93
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