SEC66/YBR171W Literature Guide Help

Other names published for SEC66: HSS1, SEC71, YBR171W

SEC66 - Protein-protein Interactions (15)

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
Spiller MP and Stirling CJ  (2011) Preferential targeting of a signal recognition particle-dependent precursor to the Ssh1p translocon in yeast. J Biol Chem 286(25):21953-60
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
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
Cosson P, et al.  (1998) New COP1-binding motifs involved in ER retrieval. EMBO J 17(23):6863-70
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
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
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