DSK2/YMR276W Literature Guide Help

Other names published for DSK2: YMR276W

DSK2 - Mutants/Phenotypes (33)

Results: 1 - 30 of 33 records
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ReferenceOther Genes Addressed
Rosenzweig R, et al.  (2012) Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome. J Biol Chem 287(18):14659-71
Dziedzic SA and Caplan AB  (2011) Identification of autophagy genes participating in zinc-induced necrotic cell death in Saccharomyces cerevisiae. Autophagy 7(5):490-500
Heinen C, et al.  (2011) C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation. Nat Commun 2():191
Inobe T, et al.  (2011) Defining the geometry of the two-component proteasome degron. Nat Chem Biol 7(3):161-7
Liu C, et al.  (2011) Ubiquitin ligase Ufd2 is required for efficient degradation of Mps1 kinase. J Biol Chem 286(51):43660-7
Sekiguchi T, et al.  (2011) Ubiquitin chains in the Dsk2 UBL domain mediate Dsk2 stability and protein degradation in yeast. Biochem Biophys Res Commun 411(3):555-61
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
Barbin L, et al.  (2010) The Cdc48-Ufd1-Npl4 complex is central in ubiquitin-proteasome triggered catabolite degradation of fructose-1,6-bisphosphatase. Biochem Biophys Res Commun 394(2):335-41
Liu C, et al.  (2010) Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates. J Biol Chem 285(14):10265-72
Zhao S and Ulrich HD  (2010) Distinct consequences of posttranslational modification by linear versus K63-linked polyubiquitin chains. Proc Natl Acad Sci U S A 107(17):7704-9
Garza RM, et al.  (2009) In vitro analysis of Hrd1p-mediated retrotranslocation of its multispanning membrane substrate 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase. J Biol Chem 284(22):14710-22
Liu C, et al.  (2009) A genome-wide synthetic dosage lethality screen reveals multiple pathways that require the functioning of ubiquitin-binding proteins Rad23 and Dsk2. BMC Biol 7(1):75
Xu P, et al.  (2009) Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137(1):133-45
Matiuhin Y, et al.  (2008) Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome. Mol Cell 32(3):415-25
Seong KM, et al.  (2007) Rpn10p is a receptor for ubiquitinated Gcn4p in proteasomal proteolysis. Mol Cells 24(2):194-9
Diaz-Martinez LA, et al.  (2006) Yeast UBL-UBA proteins have partially redundant functions in cell cycle control. Cell Div 1:28
Heiligenstein S, et al.  (2006) Retrotranslocation of a viral A/B toxin from the yeast endoplasmic reticulum is independent of ubiquitination and ERAD. EMBO J 25(20):4717-27
Kim I, et al.  (2006) The Png1-Rad23 complex regulates glycoprotein turnover. J Cell Biol 172(2):211-9
Kaplun L, et al.  (2005) The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease. Mol Cell Biol 25(13):5355-62
Ohno A, et al.  (2005) Structure of the UBA domain of Dsk2p in complex with ubiquitin molecular determinants for ubiquitin recognition. Structure 13(4):521-32
Richly H, et al.  (2005) A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120(1):73-84
Sasaki T, et al.  (2005) Budding yeast Dsk2 protein forms a homodimer via its C-terminal UBA domain. Biochem Biophys Res Commun 336(2):530-5
Elsasser S, et al.  (2004) Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome. J Biol Chem 279(26):26817-22
Funakoshi M, et al.  (2004) Sem1, the yeast ortholog of a human BRCA2-binding protein, is a component of the proteasome regulatory particle that enhances proteasome stability. J Cell Sci 117(Pt 26):6447-54
Kim I, et al.  (2004) Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis. Mol Biol Cell 15(7):3357-65
Medicherla B, et al.  (2004) A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation. EMBO Rep 5(7):692-7
Funakoshi M, et al.  (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci U S A 99(2):745-50
Rao H and Sastry A  (2002) Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23. J Biol Chem 277(14):11691-5
Saeki Y, et al.  (2002) Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochem Biophys Res Commun 293(3):986-92
Kaye FJ, et al.  (2000) A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch. FEBS Lett 467(2-3):348-55
Results: 1 - 30 of 33 records
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