Source:http://linkedlifedata.com/resource/pubmed/id/16682006
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2006-5-17
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pubmed:abstractText |
Centromere-associated protein E (CENP-E) is a kinesin-related microtubule motor protein that is essential for chromosome congression during mitosis. Our previous studies show that microtubule motor CENP-E represents a link between attachment of spindle microtubules and the mitotic checkpoint signaling cascade. However, the molecular function of CENP-E at the midbody had remained elusive. Here we show that CENP-E interacts with Skp1 at the midbody and participates in cytokinesis. CENP-E interacts with Skp1 in vitro and in vivo via its coiled-coil domain. Our yeast two-hybrid assays mapped the binding interfaces to the central stalk region of CENP-E (955-1571 aa) and the C-terminal 33 amino acids of Skp1, respectively. Our immunocytochemical studies revealed that CENP-E targets to the midbody prior to Skp1 and the midbody localization of CENP-E becomes diminished as Skp1 arrives at the midbody. Suppression of Skp1 in mitotic HeLa cells by siRNA resulted in accumulation of telophase cells with elongated inter-cell bridges and with midbodies stretched 2-3 times longer than that of normal cells. These Skp1-eliminated or -suppressed cells accumulate higher level of CENP-E, suggesting that spatiotemporal regulation of CENP-E degradation at the midbody is essential for cytokinesis. Over-expression of Skp1 lacking the CENP-E-binding domain confirmed that Skp1-CENP-E interaction is essential for faithful cytokinesis. We hypothesize that CENP-E degradation is essential for faithful mitotic exit and the proteolysis of CENP-E is mediated by SCF via a direct Skp1 link.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Motor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/S-Phase Kinase-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/centromere protein E
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-291X
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pubmed:author |
pubmed-author:CaiXinX,
pubmed-author:DouZhenZ,
pubmed-author:FengCijianC,
pubmed-author:JinChangjiangC,
pubmed-author:JosKK,
pubmed-author:LumF GFG,
pubmed-author:PuJingJ,
pubmed-author:RaiS BSB,
pubmed-author:TakeyasuKunioK,
pubmed-author:YangYeY,
pubmed-author:YaoXuebiaoX,
pubmed-author:ZhangNingN,
pubmed-author:ZhuMeiM
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
345
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
394-402
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16682006-Cell Cycle Proteins,
pubmed-meshheading:16682006-Centrosome,
pubmed-meshheading:16682006-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:16682006-Cytokinesis,
pubmed-meshheading:16682006-Molecular Motor Proteins,
pubmed-meshheading:16682006-Protein Binding,
pubmed-meshheading:16682006-Protein Interaction Mapping,
pubmed-meshheading:16682006-S-Phase Kinase-Associated Proteins
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pubmed:year |
2006
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pubmed:articleTitle |
Interaction of Skp1 with CENP-E at the midbody is essential for cytokinesis.
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pubmed:affiliation |
Division of Cellular Dynamics, Hefei National Laboratory and University of Science & Technology of China, Hefei, China 230027.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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