| pubmed-article:9060463 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9060463 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:9060463 | lifeskim:mentions | umls-concept:C1332722 | lld:lifeskim |
| pubmed-article:9060463 | lifeskim:mentions | umls-concept:C1335642 | lld:lifeskim |
| pubmed-article:9060463 | lifeskim:mentions | umls-concept:C1155689 | lld:lifeskim |
| pubmed-article:9060463 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:9060463 | lifeskim:mentions | umls-concept:C1705848 | lld:lifeskim |
| pubmed-article:9060463 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:9060463 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:9060463 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:9060463 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9060463 | pubmed:dateCreated | 1997-4-7 | lld:pubmed |
| pubmed-article:9060463 | pubmed:abstractText | The MPS1 gene from Saccharomyces cerevisiae encodes an essential protein kinase required for spindle pole body (SPB) duplication and for the mitotic spindle assembly checkpoint. Cells with the mps1-1 mutation fail early in SPB duplication and proceed through monopolar mitosis with lethal consequences. We identified CDC37 as a multicopy suppressor of mps1-1 temperature-sensitive growth. Suppression is allele specific, and synthetic lethal interactions occur between mps1 and cdc37 alleles. We examined the cdc37-1 phenotype for defects related to the SPB cycle. The cdc37-1 temperature-sensitive allele causes unbudded, G1 arrest at Start (Reed, S.I. 1980. Genetics. 95: 561-577). Reciprocal shifts demonstrate that cdc37-1 arrest is interdependent with alpha-factor arrest but is not a normal Start arrest. Although the cells are responsive to alpha-factor at the arrest, SPB duplication is uncoupled from other aspects of G1 progression and proceeds past the satellite-bearing SPB stage normally seen at Start. Electron microscopy reveals side-by-side SPBs at cdc37-1 arrest. The outer plaque of one SPB is missing or reduced, while the other is normal. Using the mps2-1 mutation to distinguish between the SPBs, we find that the outer plaque defect is specific to the new SPB. This phenotype may arise in part from reduced Mps1p function: although Mps1p protein levels are unaffected by the cdc37-1 mutation, kinase activity is markedly reduced. These data demonstrate a requirement for CDC37 in SPB duplication and suggest a role for this gene in G1 control. CDC37 may provide a chaperone function that promotes the activity of protein kinases. | lld:pubmed |
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| pubmed-article:9060463 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9060463 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9060463 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9060463 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9060463 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9060463 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9060463 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:9060463 | pubmed:author | pubmed-author:GiddingsT... | lld:pubmed |
| pubmed-article:9060463 | pubmed:author | pubmed-author:SteinerEE | lld:pubmed |
| pubmed-article:9060463 | pubmed:author | pubmed-author:WinesWW | lld:pubmed |
| pubmed-article:9060463 | pubmed:author | pubmed-author:SchutzA RAR | lld:pubmed |
| pubmed-article:9060463 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9060463 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:9060463 | pubmed:volume | 136 | lld:pubmed |
| pubmed-article:9060463 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9060463 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9060463 | pubmed:pagination | 969-82 | lld:pubmed |
| pubmed-article:9060463 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:9060463 | pubmed:meshHeading | pubmed-meshheading:9060463-... | lld:pubmed |
| pubmed-article:9060463 | pubmed:meshHeading | pubmed-meshheading:9060463-... | lld:pubmed |
| pubmed-article:9060463 | pubmed:meshHeading | pubmed-meshheading:9060463-... | lld:pubmed |
| pubmed-article:9060463 | pubmed:meshHeading | pubmed-meshheading:9060463-... | lld:pubmed |
| pubmed-article:9060463 | pubmed:meshHeading | pubmed-meshheading:9060463-... | lld:pubmed |
