DSK2/YMR276W Literature Guide Help

Other names published for DSK2: YMR276W

DSK2 - Protein-protein Interactions (27)

ReferenceOther Genes Addressed
Rosenzweig R, et al.  (2012) Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome. J Biol Chem 287(18):14659-71
Gomez TA, et al.  (2011) Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1. BMC Biol 9(1):33
Fatimababy AS, et al.  (2010) Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis. FEBS J 277(3):796-816
Hanzelmann P, et al.  (2010) The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding domain. J Biol Chem 285(26):20390-8
Kaake RM, et al.  (2010) Characterization of cell cycle specific protein interaction networks of the yeast 26S proteasome complex by the QTAX strategy. J Proteome Res 9(4):2016-29
Liu C, et al.  (2010) Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates. J Biol Chem 285(14):10265-72
Philippi A, et al.  (2010) TOR-dependent reduction in the expression level of Rrn3p lowers the activity of the yeast RNA Pol I machinery, but does not account for the strong inhibition of rRNA production. Nucleic Acids Res 38(16):5315-26
Carbonell P, et al.  (2009) Energetic determinants of protein binding specificity: insights into protein interaction networks. Proteomics 9(7):1744-53
Sims JJ, et al.  (2009) Avid interactions underlie the Lys63-linked polyubiquitin binding specificities observed for UBA domains. Nat Struct Mol Biol 16(8):883-9
Wang Y, et al.  (2009) Abnormal proteins can form aggresome in yeast: aggresome-targeting signals and components of the machinery. FASEB J 23(2):451-63
Zhang D, et al.  (2009) Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor. Mol Cell 36(6):1018-33
Guerrero C, et al.  (2008) Characterization of the proteasome interaction network using a QTAX-based tag-team strategy and protein interaction network analysis. Proc Natl Acad Sci U S A 105(36):13333-8
Matiuhin Y, et al.  (2008) Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome. Mol Cell 32(3):415-25
Ghaboosi N and Deshaies RJ  (2007) A conditional yeast e1 mutant blocks the ubiquitin-proteasome pathway and reveals a role for ubiquitin conjugates in targeting rad23 to the proteasome. Mol Biol Cell 18(5):1953-63
Guerrero C, et al.  (2006) An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network. Mol Cell Proteomics 5(2):366-78
Ishii T, et al.  (2006) Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway. EMBO J 25(23):5492-503
Apodaca J, et al.  (2005) Analysis of ubiquitin chain-binding proteins by two-hybrid methods. Methods Enzymol 399:157-64
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
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
Elsasser S, et al.  (2002) Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nat Cell Biol 4(9):725-30
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) Identification of ubiquitin-like protein-binding subunits of the 26S proteasome. Biochem Biophys Res Commun 296(4):813-9
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
Khalfan W, et al.  (2000) Functional interaction between the PKC1 pathway and CDC31 network of SPB duplication genes. Genetics 155(4):1543-59