http://purl.uniprot.org/citations/9736614 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9736614 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/9736614 | http://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/9736614 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/17.18.5360"xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/17.18.5360"xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/author | "Peter M."xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/author | "Peter M."xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/author | "Jaquenoud M."xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/author | "Jaquenoud M."xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/author | "Gulli M.P."xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/author | "Gulli M.P."xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/author | "Peter K."xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/author | "Peter K."xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/pages | "5360-5373"xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/pages | "5360-5373"xsd:string |
http://purl.uniprot.org/citations/9736614 | http://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/9736614 | http://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/9736614 | http://purl.uniprot.org/core/volume | "17"xsd:string |
http://purl.uniprot.org/citations/9736614 | http://purl.uniprot.org/core/volume | "17"xsd:string |
http://purl.uniprot.org/citations/9736614 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9736614 |
http://purl.uniprot.org/citations/9736614 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9736614 |