| pubmed-article:11113154 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11113154 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:11113154 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:11113154 | lifeskim:mentions | umls-concept:C0120465 | lld:lifeskim |
| pubmed-article:11113154 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:11113154 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:11113154 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:11113154 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:11113154 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:11113154 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:11113154 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:11113154 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:11113154 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:11113154 | pubmed:dateCreated | 2001-5-25 | lld:pubmed |
| pubmed-article:11113154 | pubmed:abstractText | In budding yeast cells, the cytoskeletal polarization and depolarization events that shape the bud are triggered at specific times during the cell cycle by the cyclin-dependent kinase Cdc28p. Polarity establishment also requires the small GTPase Cdc42p and its exchange factor, Cdc24p, but the mechanism whereby Cdc28p induces Cdc42p-dependent polarization is unknown. Here we show that Cdc24p becomes phosphorylated in a cell cycle-dependent manner, triggered by Cdc28p. However, the role of Cdc28p is indirect, and the phosphorylation appears to be catalyzed by the p21-activated kinase family member Cla4p and also depends on Cdc42p and the scaffold protein Bem1p. Expression of GTP-Cdc42p, the product of Cdc24p-mediated GDP/GTP exchange, stimulated Cdc24p phosphorylation independent of cell cycle cues, raising the possibility that the phosphorylation is part of a feedback regulatory pathway. Bem1p binds directly to Cdc24p, to Cla4p, and to GTP-bound Cdc42p and can mediate complex formation between these proteins in vitro. We suggest that Bem1p acts to concentrate polarity establishment proteins at a discrete site, facilitating polarization and promoting Cdc24p phosphorylation at specific times during the cell cycle. | lld:pubmed |
| pubmed-article:11113154 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113154 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11113154 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113154 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11113154 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113154 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11113154 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11113154 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113154 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113154 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113154 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11113154 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11113154 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11113154 | pubmed:author | pubmed-author:DeoL RLR | lld:pubmed |
| pubmed-article:11113154 | pubmed:author | pubmed-author:BorgTT | lld:pubmed |
| pubmed-article:11113154 | pubmed:author | pubmed-author:MoskowJ JJJ | lld:pubmed |
| pubmed-article:11113154 | pubmed:author | pubmed-author:BardesE SES | lld:pubmed |
| pubmed-article:11113154 | pubmed:author | pubmed-author:IrazoquiJ EJE | lld:pubmed |
| pubmed-article:11113154 | pubmed:author | pubmed-author:ZylaT RTR | lld:pubmed |
| pubmed-article:11113154 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11113154 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:11113154 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:11113154 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11113154 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11113154 | pubmed:pagination | 7176-86 | lld:pubmed |
| pubmed-article:11113154 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:11113154 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11113154 | pubmed:articleTitle | Assembly of scaffold-mediated complexes containing Cdc42p, the exchange factor Cdc24p, and the effector Cla4p required for cell cycle-regulated phosphorylation of Cdc24p. | lld:pubmed |
| pubmed-article:11113154 | pubmed:affiliation | Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710, USA. | lld:pubmed |
| pubmed-article:11113154 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11113154 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11113154 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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