YOS9/YDR057W Literature Guide Help

Other names published for YOS9: YDR057W

YOS9 - Mutants/Phenotypes (22)

ReferenceOther Genes Addressed
Hanna J, et al.  (2012) Structural and biochemical basis of Yos9 protein dimerization and possible contribution to self-association of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation ubiquitin-ligase complex. J Biol Chem 287(11):8633-40
Huttner S, et al.  (2012) Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic reticulum-associated degradation of glycoproteins. Plant Mol Biol 79(1-2):21-33
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
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
Benitez EM, et al.  (2011) Yos9, a control protein for misfolded glycosylated and non-glycosylated proteins in ERAD. FEBS Lett 585(19):3015-9
Chantret I, et al.  (2011) Endoplasmic reticulum-associated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae. J Biol Chem 286(48):41786-800
Villa-Garcia MJ, et al.  (2011) Genome-wide screen for inositol auxotrophy in Saccharomyces cerevisiae implicates lipid metabolism in stress response signaling. Mol Genet Genomics 285(2):125-49
Carvalho P, et al.  (2010) Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p. Cell 143(4):579-91
Hosomi A, et al.  (2010) Identification of an Htm1 (EDEM)-dependent, Mns1-independent Endoplasmic Reticulum-associated Degradation (ERAD) Pathway in Saccharomyces cerevisiae: APPLICATION OF A NOVEL ASSAY FOR GLYCOPROTEIN ERAD. J Biol Chem 285(32):24324-34
Kanehara K, et al.  (2010) Modularity of the Hrd1 ERAD complex underlies its diverse client range. J Cell Biol 188(5):707-16
Clerc S, et al.  (2009) Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. J Cell Biol 184(1):159-72
Horn SC, et al.  (2009) Usa1 functions as a scaffold of the HRD-ubiquitin ligase. Mol Cell 36(5):782-93
Jonikas MC, et al.  (2009) Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science 323(5922):1693-7
Sato BK, et al.  (2009) Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase. Mol Cell 34(2):212-22
Quan EM, et al.  (2008) Defining the glycan destruction signal for endoplasmic reticulum-associated degradation. Mol Cell 32(6):870-7
Denic V, et al.  (2006) A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 126(2):349-59
Bhamidipati A, et al.  (2005) Exploration of the Topological Requirements of ERAD Identifies Yos9p as a Lectin Sensor of Misfolded Glycoproteins in the ER Lumen. Mol Cell 19(6):741-51
Kim W, et al.  (2005) Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol Cell 19(6):753-64
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
Buschhorn BA, et al.  (2004) A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins. FEBS Lett 577(3):422-6
Friedmann E, et al.  (2002) YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins. J Biol Chem 277(38):35274-81