CDC34/YDR054C Literature Guide Help

Other names published for CDC34: DNA6, UBC3, SCF E2 ubiquitin-protein ligase catalytic subunit CDC34, YDR054C

CDC34 - Protein-protein Interactions (24)

ReferenceOther Genes Addressed
Doris KS, et al.  (2012) Oxidative stress responses involve oxidation of a conserved ubiquitin pathway enzyme. Mol Cell Biol 32(21):4472-81
Kleiger G, et al.  (2009) Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates. Cell 139(5):957-68
Liu Y, et al.  (2009) A longevity protein, Lag2, interacts with SCF complex and regulates SCF function. EMBO J 28(21):3366-77
Li Z, et al.  (2008) Cdc34p Ubiquitin-Conjugating Enzyme Is a Component of the Tombusvirus Replicase Complex and Ubiquitinates p33 Replication Protein. J Virol 82(14):6911-26
Takahashi S, et al.  (2008) Upf1 potentially serves as a RING-related E3 ubiquitin ligase via its association with Upf3 in yeast. RNA 14(9):1950-8
Zaidi IW, et al.  (2008) Rtt101 and Mms1 in budding yeast form a CUL4(DDB1)-like ubiquitin ligase that promotes replication through damaged DNA. EMBO Rep 9(10):1034-40
Wu X, et al.  (2006) Prediction of yeast protein-protein interaction network: insights from the Gene Ontology and annotations. Nucleic Acids Res 34(7):2137-50
Flick K, et al.  (2004) Proteolysis-independent regulation of the transcription factor Met4 by a single Lys 48-linked ubiquitin chain. Nat Cell Biol 6(7):634-41
Kus BM, et al.  (2004) Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro. Proteins 54(3):455-67
Deffenbaugh AE, et al.  (2003) Release of ubiquitin-charged Cdc34-S - Ub from the RING domain is essential for ubiquitination of the SCF(Cdc4)-bound substrate Sic1. Cell 114(5):611-22
Varelas X, et al.  (2003) Cdc34 self-association is facilitated by ubiquitin thiolester formation and is required for its catalytic activity. Mol Cell Biol 23(15):5388-400
Jaquenoud M, et al.  (2002) Cell cycle-dependent nuclear export of Cdh1p may contribute to the inactivation of APC/C(Cdh1). EMBO J 21(23):6515-26
Blondel M, et al.  (2000) Isolation and characterization of HRT1 using a genetic screen for mutants unable to degrade Gic2p in saccharomyces cerevisiae. Genetics 155(3):1033-44
Kaiser P, et al.  (2000) Regulation of transcription by ubiquitination without proteolysis: Cdc34/SCF(Met30)-mediated inactivation of the transcription factor Met4. Cell 102(3):303-14
Rouillon A, et al.  (2000) Feedback-regulated degradation of the transcriptional activator Met4 is triggered by the SCF(Met30 )complex. EMBO J 19(2):282-94
Smothers DB, et al.  (2000) The abundance of Met30p limits SCF(Met30p) complex activity and is regulated by methionine availability. Mol Cell Biol 20(21):7845-52
Galan JM and Peter M  (1999) Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism. Proc Natl Acad Sci U S A 96(16):9124-9
Skowyra D, et al.  (1999) Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1. Science 284(5414):662-5
Willems AR, et al.  (1999) SCF ubiquitin protein ligases and phosphorylation-dependent proteolysis. Philos Trans R Soc Lond B Biol Sci 354(1389):1533-50
Kishi T and Yamao F  (1998) An essential function of Grr1 for the degradation of Cln2 is to act as a binding core that links Cln2 to Skp1. J Cell Sci 111 ( Pt 24):3655-61
Patton EE, et al.  (1998) Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box proteincomplexes that regulate cell division and methionine biosynthesis in yeast. Genes Dev 12(5):692-705
Skowyra D, et al.  (1997) F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91(2):209-19
Willems AR, et al.  (1996) Cdc53 targets phosphorylated G1 cyclins for degradation by the ubiquitin proteolytic pathway. Cell 86(3):453-63
Ptak C, et al.  (1994) Functional and physical characterization of the cell cycle ubiquitin-conjugating enzyme CDC34 (UBC3). Identification of a functional determinant within the tail that facilitates CDC34 self-association. J Biol Chem 269(42):26539-45