PEP1/YBL017C Literature Guide Help

Other names published for PEP1: VPS10, VPT1, YBL017C

PEP1 - Function/Process (23)

ReferenceOther Genes Addressed
Kruse KB, et al.  (2006) Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ. Mol Biol Cell 17(1):203-12
Takegawa K, et al.  (2003) Heterologous expression and characterization of Schizosaccharomyces pombe vacuolar carboxypeptidase Y in Saccharomyces cerevisiae. Curr Genet 42(5):252-9
Deloche O and Schekman RW  (2002) Vps10p cycles between the TGN and the late endosome via the plasma membrane in clathrin mutants. Mol Biol Cell 13(12):4296-307
Dennes A, et al.  (2002) The yeast Vps10p cytoplasmic tail mediates lysosomal sorting in mammalian cells and interacts with human GGAs. J Biol Chem 277(14):12288-93
Harsay E and Schekman R  (2002) A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway. J Cell Biol 156(2):271-85
Bensen ES, et al.  (2001) Ric1p and the Ypt6p GTPase function in a common pathway required for localization of trans-Golgi network membrane proteins. Mol Biol Cell 12(1):13-26
Deloche O, et al.  (2001) Vps10p transport from the trans-Golgi network to the endosome is mediated by clathrin-coated vesicles. Mol Biol Cell 12(2):475-85
Poon PP, et al.  (2001) The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function for transport from the yeast trans-Golgi network. J Cell Biol 155(7):1239-50
Reddy JV and Seaman MN  (2001) Vps26p, a component of retromer, directs the interactions of Vps35p in endosome-to-Golgi retrieval. Mol Biol Cell 12(10):3242-56
Whyte JR and Munro S  (2001) A yeast homolog of the mammalian mannose 6-phosphate receptors contributes to the sorting of vacuolar hydrolases. Curr Biol 11(13):1074-8
Zhang By, et al.  (2001) Intracellular retention of newly synthesized insulin in yeast is caused by endoproteolytic processing in the Golgi complex. J Cell Biol 153(6):1187-98
Gerrard SR, et al.  (2000) VPS21 controls entry of endocytosed and biosynthetic proteins into the yeast prevacuolar compartment. Mol Biol Cell 11(2):613-26
Jorgensen MU, et al.  (1999) Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae. Eur J Biochem 260(2):461-9
Holkeri H and Makarow M  (1998) Different degradation pathways for heterologous glycoproteins in yeast. FEBS Lett 429(2):162-6
Horazdovsky BF, et al.  (1997) A sorting nexin-1 homologue, Vps5p, forms a complex with Vps17p and is required for recycling the vacuolar protein-sorting receptor. Mol Biol Cell 8(8):1529-41
Seaman MN, et al.  (1997) Endosome to Golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the VPS29, VPS30, and VPS35 gene products. J Cell Biol 137(1):79-92
Cooper AA and Stevens TH  (1996) Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases. J Cell Biol 133(3):529-41
Westphal V, et al.  (1996) Multiple pathways for vacuolar sorting of yeast proteinase A. J Biol Chem 271(20):11865-70
Cereghino JL, et al.  (1995) The cytoplasmic tail domain of the vacuolar protein sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function, and localization. Mol Biol Cell 6(9):1089-102
Stack JH, et al.  (1995) Novel protein kinase/phosphatidylinositol 3-kinase complex essential for receptor-mediated protein sorting to the vacuole in yeast. Cold Spring Harb Symp Quant Biol 60():157-70
Marcusson EG, et al.  (1994) The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene. Cell 77(4):579-86
Robinson JS, et al.  (1988) Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol Cell Biol 8(11):4936-48
Bankaitis VA, et al.  (1986) Isolation of yeast mutants defective in protein targeting to the vacuole. Proc Natl Acad Sci U S A 83(23):9075-9