| pubmed-article:9430641 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9430641 | lifeskim:mentions | umls-concept:C0014181 | lld:lifeskim |
| pubmed-article:9430641 | lifeskim:mentions | umls-concept:C0162832 | lld:lifeskim |
| pubmed-article:9430641 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:9430641 | lifeskim:mentions | umls-concept:C1332100 | lld:lifeskim |
| pubmed-article:9430641 | lifeskim:mentions | umls-concept:C1704686 | lld:lifeskim |
| pubmed-article:9430641 | lifeskim:mentions | umls-concept:C1622911 | lld:lifeskim |
| pubmed-article:9430641 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:9430641 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
| pubmed-article:9430641 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:9430641 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:9430641 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9430641 | pubmed:dateCreated | 1998-2-26 | lld:pubmed |
| pubmed-article:9430641 | pubmed:abstractText | SIC1 is a non-essential gene encoding a CDK inhibitor of Cdc28-Clb kinase activity. Sic1p is involved in both mitotic exit and the timing of DNA synthesis. To identify other genes involved in controlling Clb-kinase activity, we have undertaken a genetic screen for mutations which render SIC1 essential. Here we describe a gene we have identified by this means, RSI1/APC2. Temperature-sensitive rsi1/apc2 mutants arrest in metaphase and are unable to degrade Clb2p, suggesting that Rsi1p/Apc2p is associated with the anaphase promoting complex (APC). This is an E3 ubiquitin-ligase that controls anaphase initiation through degradation of Pds1p and mitotic exit via degradation of Clb cyclins. Indeed, the anaphase block in rsi1/apc2 temperature-sensitive mutants is overcome by removal of PDS1, consistent with Rsi1p/Apc2p being part of the APC. In addition, like our rsi1/apc2 mutations, cdc23-1, encoding a known APC subunit, is also lethal with sic1Delta. Thus SIC1 clearly becomes essential when APC function is compromised. Finally, we find that Rsi1p/Apc2p co-immunoprecipitates with Cdc23p. Taken together, our results suggest that RSI1/APC2 is a subunit of APC. | lld:pubmed |
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| pubmed-article:9430641 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9430641 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9430641 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9430641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9430641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9430641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9430641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9430641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9430641 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9430641 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:9430641 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:9430641 | pubmed:author | pubmed-author:JohnsonA LAL | lld:pubmed |
| pubmed-article:9430641 | pubmed:author | pubmed-author:JohnstonL HLH | lld:pubmed |
| pubmed-article:9430641 | pubmed:author | pubmed-author:FesquetDD | lld:pubmed |
| pubmed-article:9430641 | pubmed:author | pubmed-author:KramerK MKM | lld:pubmed |
| pubmed-article:9430641 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9430641 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9430641 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:9430641 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9430641 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9430641 | pubmed:pagination | 498-506 | lld:pubmed |
| pubmed-article:9430641 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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