SEC72/YLR292C Literature Guide Help

Other names published for SEC72: SEC67, SIM2, YLR292C

SEC72 - Function/Process (14)

ReferenceOther Genes Addressed
Schuldiner M, et al.  (2005) Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell 123(3):507-19
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
Brizzio V, et al.  (1999) Genetic interactions between KAR7/SEC71, KAR8/JEM1, KAR5, and KAR2 during nuclear fusion in Saccharomyces cerevisiae. Mol Biol Cell 10(3):609-26
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
Lyman SK and Schekman R  (1996) Polypeptide translocation machinery of the yeast endoplasmic reticulum. Experientia 52(12):1042-9
Ng DT and Walter P  (1996) ER membrane protein complex required for nuclear fusion. J Cell Biol 132(4):499-509
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
Feldheim D and Schekman R  (1994) Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex. J Cell Biol 126(4):935-43
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