SEC72/YLR292C Literature Guide Help

Other names published for SEC72: SEC67, SIM2, YLR292C

SEC72 - Protein-protein Interactions (15)

ReferenceOther Genes Addressed
Kim KH, et al.  (2012) Novel beta-structure of YLR301w from Saccharomyces cerevisiae. Acta Crystallogr D Biol Crystallogr 68(Pt 5):531-40
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
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
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
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
Panzner S, et al.  (1995) Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81(4):561-70
Fang H and Green N  (1994) Nonlethal sec71-1 and sec72-1 mutations eliminate proteins associated with the Sec63p-BiP complex from S. cerevisiae. Mol Biol Cell 5(9):933-42
Brodsky JL and Schekman R  (1993) A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J Cell Biol 123(6 Pt 1):1355-63