KAR2/YJL034W Literature Guide Help

Other names published for KAR2: GRP78, BIP, Hsp70 family ATPase KAR2, YJL034W

KAR2 - Substrates/Ligands/Cofactors (18)

ReferenceOther Genes Addressed
Hsu CL, et al.  (2012) Endoplasmic reticulum stress regulation of the Kar2p/BiP chaperone alleviates proteotoxicity via dual degradation pathways. Mol Biol Cell 23(4):630-41
Lajoie P, et al.  (2012) Kar2p availability defines distinct forms of endoplasmic reticulum stress in living cells. Mol Biol Cell 23(5):955-64
Yan M, et al.  (2011) Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor. Biochem J 438(3):447-55
Hale SJ, et al.  (2010) Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct. J Biol Chem 285(28):21600-6
Kanehara K, et al.  (2010) Modularity of the Hrd1 ERAD complex underlies its diverse client range. J Cell Biol 188(5):707-16
Xie W, et al.  (2009) Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation system. Mol Biol Cell 20(14):3317-29
Todd-Corlett A, et al.  (2007) Lobe IB of the ATPase domain of Kar2p/BiP interacts with Ire1p to negatively regulate the unfolded protein response in Saccharomyces cerevisiae. J Mol Biol 367(3):770-87
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
Taxis C, et al.  (2003) Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD. J Biol Chem 278(38):35903-13
Fewell SW, et al.  (2001) Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis. J Biol Chem 276(2):910-4
Amshoff C, et al.  (1999) Cycloheximide, a new tool to dissect specific steps in ER-associated degradation of different substrates. Biol Chem 380(6):669-77
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
Lopez-Buesa P, et al.  (1998) The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains. Proc Natl Acad Sci U S A 95(26):15253-8
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
King C, et al.  (1995) Polymerization of 70-kDa heat shock protein by yeast DnaJ in ATP. J Biol Chem 270(38):22535-40
Flynn GC, et al.  (1991) Peptide-binding specificity of the molecular chaperone BiP. Nature 353(6346):726-30