PRC1/YMR297W Literature Guide Help

Other names published for PRC1: LBC1, CPY, carboxypeptidase C PRC1, YMR297W

PRC1 - Protein-protein Interactions (16)

ReferenceOther Genes Addressed
Beaufour M, et al.  (2012) Interaction proteomics suggests a new role for the Tfs1 protein in yeast. J Proteome Res ()
Grubb S, et al.  (2012) Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates. Mol Biol Cell 23(4):520-32
Izawa T, et al.  (2012) Roles of dom34:hbs1 in nonstop protein clearance from translocators for normal organelle protein influx. Cell Rep 2(3):447-53
Izawa T, et al.  (2012) Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation. Mol Biol Cell 23(7):1283-93
Gardner BM and Walter P  (2011) Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response. Science 333(6051):1891-4
Ishiwata-Kimata Y, et al.  (2011) Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways. Mol Biol Cell 22(18):3520-32
Kincaid MM and Cooper AA  (2007) Misfolded proteins traffic from the endoplasmic reticulum (ER) due to ER export signals. Mol Biol Cell 18(2):455-63
Szathmary R, et al.  (2005) Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol Cell 19(6):765-75
Mima J, et al.  (2003) The multiple site binding of carboxypeptidase Y inhibitor (IC) to the cognate proteinase. Implications for the biological roles of the phosphatidylethanolamine-binding protein. J Biol Chem 278(32):29792-8
Takegawa K, et al.  (2003) Heterologous expression and characterization of Schizosaccharomyces pombe vacuolar carboxypeptidase Y in Saccharomyces cerevisiae. Curr Genet 42(5):252-9
Mima J, et al.  (2002) N-terminal acetyl group is essential for the inhibitory function of carboxypeptidase Y inhibitor (I(C)). FEBS Lett 532(1-2):207-10
Mima J, et al.  (2002) Overexpression and functional characterization of a serine carboxypeptidase inhibitor (I(C)) from Saccharomyces cerevisiae. J Biochem 132(6):967-73
Wittke S, et al.  (2002) Recognition of a subset of signal sequences by Ssh1p, a Sec61p-related protein in the membrane of endoplasmic reticulum of yeast Saccharomyces cerevisiae. Mol Biol Cell 13(7):2223-32
Marcusson EG, et al.  (1994) The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene. Cell 77(4):579-86
te Heesen S and Aebi M  (1994) The genetic interaction of kar2 and wbp1 mutations. Distinct functions of binding protein BiP and N-linked glycosylation in the processing pathway of secreted proteins in Saccharomyces cerevisiae. Eur J Biochem 222(2):631-7
Stevens TH, et al.  (1986) Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y. J Cell Biol 102(5):1551-7