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http://purl.uniprot.org/citations/9736614http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9736614http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9736614http://www.w3.org/2000/01/rdf-schema#comment"Cdc42p, a Rho-related GTP-binding protein, regulates cytoskeletal polarization and rearrangements in eukaryotic cells. In yeast, Gic1p and Gic2p are effectors of Cdc42p involved in actin polarization at bud emergence. Gic2p is expressed in a cell cycle-dependent manner and rapidly disappears shortly after bud emergence concomitant with the activation of the G1 cyclin-dependent kinase Cdc28p-Clnp. Here we have shown that the rapid disappearance of Gic2p results from ubiquitin-dependent proteolysis. Biochemical and genetic evidence demonstrates that degradation of Gic2p required the Skp1-cullin-F-box protein complex (SCF) components Cdc34p, Cdc53p, Skp1p and Grr1p, but not Cdc4p. Phosphorylation of several C-terminal sites of Gic2p served as part of the recognition signal for ubiquitination. In addition, binding of Gic2p to Cdc42p was a prerequisite for degradation, suggesting that specifically the active form of Gic2p is targeted for destruction. Finally, our data indicate that degradation of Gic2p may be part of a mechanism which restricts cytoskeletal polarization in the G1 phase of the cell cycle."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.org/dc/terms/identifier"doi:10.1093/emboj/17.18.5360"xsd:string
http://purl.uniprot.org/citations/9736614http://purl.org/dc/terms/identifier"doi:10.1093/emboj/17.18.5360"xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/author"Peter M."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/author"Peter M."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/author"Jaquenoud M."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/author"Jaquenoud M."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/author"Gulli M.P."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/author"Gulli M.P."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/author"Peter K."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/author"Peter K."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/pages"5360-5373"xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/pages"5360-5373"xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/title"The Cdc42p effector Gic2p is targeted for ubiquitin-dependent degradation by the SCFGrr1 complex."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/title"The Cdc42p effector Gic2p is targeted for ubiquitin-dependent degradation by the SCFGrr1 complex."xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/9736614http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/9736614http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9736614
http://purl.uniprot.org/citations/9736614http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9736614