| pubmed-article:18022565 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18022565 | lifeskim:mentions | umls-concept:C0290178 | lld:lifeskim |
| pubmed-article:18022565 | lifeskim:mentions | umls-concept:C1335227 | lld:lifeskim |
| pubmed-article:18022565 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:18022565 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:18022565 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:18022565 | lifeskim:mentions | umls-concept:C0449445 | lld:lifeskim |
| pubmed-article:18022565 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:18022565 | pubmed:dateCreated | 2007-11-20 | lld:pubmed |
| pubmed-article:18022565 | pubmed:abstractText | Protein phosphorylation is a ubiquitous mechanism for cellular signal propagation, and signaling network complexity presents a challenge to protein kinase substrate identification. Few targets of Polo-like kinases are known, despite their significant role in coordinating cell-cycle progression. Here, we combine chemical-genetic, bioinformatic, and proteomic tools for Polo-like kinase substrate identification. Specific pharmacological inhibition of budding yeast Polo-like kinase, Cdc5, resulted in a misaligned preanaphase spindle and subsequently delayed anaphase nuclear migration, revealing a Cdc5 function. A cellular screen for Cdc5 substrates identified Spc72, a spindle pole body (SPB) component and microtubule anchor required for nuclear positioning. Spc72 bound to the Cdc5 PBD in a mitosis-specific manner, was phosphorylated by Cdc5 in vitro, and demonstrated a loss of mitotic phosphorylation in vivo upon Cdc5 inhibition. Finally, an examination of Cdc5 binding by SPB-localized proteins expanded our knowledge of Cdc5 function at the SPB. | lld:pubmed |
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| pubmed-article:18022565 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18022565 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18022565 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18022565 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18022565 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18022565 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:18022565 | pubmed:issn | 1074-5521 | lld:pubmed |
| pubmed-article:18022565 | pubmed:author | pubmed-author:ZhangChaoC | lld:pubmed |
| pubmed-article:18022565 | pubmed:author | pubmed-author:YaffeMichael... | lld:pubmed |
| pubmed-article:18022565 | pubmed:author | pubmed-author:TauntonJackJ | lld:pubmed |
| pubmed-article:18022565 | pubmed:author | pubmed-author:ShokatKevan... | lld:pubmed |
| pubmed-article:18022565 | pubmed:author | pubmed-author:CohenMichael... | lld:pubmed |
| pubmed-article:18022565 | pubmed:author | pubmed-author:MorganDavid... | lld:pubmed |
| pubmed-article:18022565 | pubmed:author | pubmed-author:LoweryDrew... | lld:pubmed |
| pubmed-article:18022565 | pubmed:author | pubmed-author:SullivanMatth... | lld:pubmed |
| pubmed-article:18022565 | pubmed:author | pubmed-author:SneadJennifer... | lld:pubmed |
| pubmed-article:18022565 | pubmed:author | pubmed-author:RandleDavid... | lld:pubmed |
| pubmed-article:18022565 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18022565 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:18022565 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18022565 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18022565 | pubmed:pagination | 1261-72 | lld:pubmed |
