UBC7/YMR022W Literature Guide Help

Other names published for UBC7: QRI8, DER2, E2 ubiquitin-conjugating protein UBC7, YMR022W

UBC7 - Genetic Interactions (32)

ReferenceOther Genes Addressed
Kurita T, et al.  (2012) Action of multiple endoplasmic reticulum chaperon-like proteins is required for proper folding and polarized localization of Kre6 protein essential in yeast cell wall ?-1,6-glucan synthesis. J Biol Chem 287(21):17415-24
Mitchell DA, et al.  (2012) The Erf4 subunit of the yeast Ras palmitoyl acyltransferase is required for stability of the Acyl-Erf2 intermediate and palmitoyl transfer to a Ras2 substrate. J Biol Chem 287(41):34337-48
Rubenstein EM, et al.  (2012) Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase. J Cell Biol 197(6):761-73
Kreft SG and Hochstrasser M  (2011) An unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzyme. J Biol Chem 286(23):20163-74
Wang Y, et al.  (2011) Ubiquitin-dependent Proteasomal Degradation of Human Liver Cytochrome P450 2E1: IDENTIFICATION OF SITES TARGETED FOR PHOSPHORYLATION AND UBIQUITINATION. J Biol Chem 286(11):9443-56
Carvalho P, et al.  (2010) Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p. Cell 143(4):579-91
Haworth J, et al.  (2010) Ubc4 and Not4 Regulate Steady-State Levels of DNA Polymerase-{alpha} to Promote Efficient and Accurate DNA Replication. Mol Biol Cell 21(18):3205-19
Jonikas MC, et al.  (2009) Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science 323(5922):1693-7
Metzger MB and Michaelis S  (2009) Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins. Mol Biol Cell 20(3):1006-19
Scrimale T, et al.  (2009) The Unfolded Protein Response Is Induced by the Cell Wall Integrity Mitogen-activated Protein Kinase Signaling Cascade and Is Required for Cell Wall Integrity in Saccharomyces cerevisiae. Mol Biol Cell 20(1):164-75
Wang Z and Prelich G  (2009) Quality control of a transcriptional regulator by SUMO-targeted degradation. Mol Cell Biol 29(7):1694-706
Duennwald ML and Lindquist S  (2008) Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev 22(23):3308-3319
Nakatsukasa K, et al.  (2008) Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell 132(1):101-12
Takeuchi M, et al.  (2008) Saccharomyces cerevisiae Rot1 Is an Essential Molecular Chaperone in the Endoplasmic Reticulum. Mol Biol Cell 19(8):3514-25
Braun S and Jentsch S  (2007) SM-protein-controlled ER-associated degradation discriminates between different SNAREs. EMBO Rep 8(12):1176-82
Kota J, et al.  (2007) Membrane chaperone Shr3 assists in folding amino acid permeases preventing precocious ERAD. J Cell Biol 176(5):617-28
Mazon MJ, et al.  (2007) Efficient degradation of misfolded mutant Pma1 by endoplasmic reticulum-associated degradation requires Atg19 and the Cvt/autophagy pathway. Mol Microbiol 63(4):1069-1077
Pagant S, et al.  (2007) Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal. Mol Biol Cell 18(9):3398-413
Loertscher J, et al.  (2006) Endoplasmic reticulum-associated degradation is required for cold adaptation and regulation of sterol biosynthesis in the yeast Saccharomyces cerevisiae. Eukaryot Cell 5(4):712-22
Arnason TG, et al.  (2005) Novel interaction between Apc5p and Rsp5p in an intracellular signaling pathway in Saccharomyces cerevisiae. Eukaryot Cell 4(1):134-46
Kiel JA, et al.  (2005) Ubiquitination of the peroxisomal targeting signal type 1 receptor, Pex5p, suggests the presence of a quality control mechanism during peroxisomal matrix protein import. J Biol Chem 280(3):1921-30
Parsons AB, et al.  (2004) Integration of chemical-genetic and genetic interaction data links bioactive compounds to cellular target pathways. Nat Biotechnol 22(1):62-9
Hitchcock AL, et al.  (2003) A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery. Proc Natl Acad Sci U S A 100(22):12735-40
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
Jarosch E, et al.  (2002) Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4(2):134-9
McBratney S and Winey M  (2002) Mutant membrane protein of the budding yeast spindle pole body is targeted to the endoplasmic reticulum degradation pathway. Genetics 162(2):567-78
Friedlander R, et al.  (2000) A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol 2(7):379-84
Ng DT, et al.  (2000) The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control. J Cell Biol 150(1):77-88
Gilon T, et al.  (1998) Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae. EMBO J 17(10):2759-66
Biederer T, et al.  (1997) Role of Cue1p in ubiquitination and degradation at the ER surface. Science 278(5344):1806-9