Other names published for PEP1: VPS10, VPT1, YBL017C
PEP1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Cellular Location
- Function/Process
- Genetic Interactions
- Mutants/Phenotypes
- Regulation of
- Regulatory Role
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
PEP1 - Cellular Location (31)
| Reference | Other Genes Addressed |
|---|---|
| Gharakhanian E, et al. (2011) env1 Mutant of VPS35 gene exhibits unique protein localization and processing phenotype at Golgi and lysosomal vacuole in Saccharomyces cerevisiae. Mol Cell Biochem 346(1-2):187-95 | |
| Nickerson DP, et al. (2010) Regulators of Vps4 ATPase activity at endosomes differentially influence the size and rate of formation of intralumenal vesicles. Mol Biol Cell 21(6):1023-32 | |
| Abazeed ME and Fuller RS (2008) Yeast golgi-localized, gamma-Ear-containing, ADP-ribosylation factor-binding proteins are but adaptor protein-1 is not required for cell-free transport of membrane proteins from the trans-golgi network to the prevacuolar compartment. Mol Biol Cell 19(11):4826-36 | |
| Chang J, et al. (2008) Purification of yeast membranes and organelles by sucrose density gradient centrifugation. Methods Mol Biol 457:141-9 | |
| Morishita M and Engebrecht J (2008) Sorting signals within the Saccharomyces cerevisiae sporulation-specific dityrosine transporter, Dtr1p, C terminus promote Golgi-to-prospore membrane transport. Eukaryot Cell 7(10):1674-84 | |
| Puria R, et al. (2008) Nuclear translocation of Gln3 in response to nutrient signals requires Golgi-to-endosome trafficking in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 105(20):7194-9 | |
| Kama R, et al. (2007) Btn2, a hook1 ortholog and potential batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast. Mol Cell Biol 27(2):605-21 | |
| Inadome H, et al. (2005) Immunoisolaton of the yeast Golgi subcompartments and characterization of a novel membrane protein, Svp26, discovered in the Sed5-containing compartments. Mol Cell Biol 25(17):7696-710 | |
| Zhang S, et al. (2004) Ncr1p, the yeast ortholog of mammalian Niemann Pick C1 protein, is dispensable for endocytic transport. Traffic 5(12):1017-30 | |
| Burda P, et al. (2002) Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase. J Cell Sci 115(Pt 20):3889-900 | |
| 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 | |
| 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 | |
| Ha SA, et al. (2001) A novel mechanism for localizing membrane proteins to yeast trans-Golgi network requires function of synaptojanin-like protein. Mol Biol Cell 12(10):3175-90 | |
| 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 | |
| Urbanowski JL and Piper RC (2001) Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole. Traffic 2(9):622-30 | |
| Edgar AJ and Polak JM (2000) Human homologues of yeast vacuolar protein sorting 29 and 35. Biochem Biophys Res Commun 277(3):622-30 | |
| Nothwehr SF, et al. (2000) Sorting of yeast membrane proteins into an endosome-to-Golgi pathway involves direct interaction of their cytosolic domains with Vps35p. J Cell Biol 151(2):297-310 | |
| Nothwehr SF, et al. (1999) Distinct domains within Vps35p mediate the retrieval of two different cargo proteins from the yeast prevacuolar/endosomal compartment. Mol Biol Cell 10(4):875-90 | |
| Spelbrink RG and Nothwehr SF (1999) The yeast GRD20 gene is required for protein sorting in the trans-Golgi network/endosomal system and for polarization of the actin cytoskeleton. Mol Biol Cell 10(12):4263-81 | |
| Kametaka S, et al. (1998) Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae. J Biol Chem 273(35):22284-91 | |
| Seaman MN, et al. (1998) A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. J Cell Biol 142(3):665-81 | |
| 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 | |
| Luo W and Chang A (1997) Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant. J Cell Biol 138(4):731-46 | |
| Nothwehr SF and Hindes AE (1997) The yeast VPS5/GRD2 gene encodes a sorting nexin-1-like protein required for localizing membrane proteins to the late Golgi. J Cell Sci 110 ( Pt 9)():1063-72 | |
| 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 | |
| Chen YJ and Stevens TH (1996) The VPS8 gene is required for localization and trafficking of the CPY sorting receptor in Saccharomyces cerevisiae. Eur J Cell Biol 70(4):289-97 | |
| 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 | |
| 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 | |
| Piper RC, et al. (1995) VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae. J Cell Biol 131(3):603-17 |





