|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
2010-4-20
|
|
pubmed:abstractText |
The formation of functional kinetochores requires the accurate assembly of a large number of protein complexes. The Hsp90-Sgt1 chaperone complex is important for this process; however, its targets are not conserved and its exact contribution to kinetochore assembly is unclear. Here, we show that human Hsp90-Sgt1 interacts with the Mis12 complex, a so-called keystone complex required to assemble a large fraction of the kinetochore. Inhibition of Hsp90 or Sgt1 destabilizes the Mis12 complex and delays proper chromosome alignment due to inefficient formation of microtubule-binding sites. Interestingly, coinhibition of Sgt1 and the SCF subunit, Skp1, increases Mis12 complexes at kinetochores and restores timely chromosome alignment but forms less-robust microtubule-binding sites. We propose that a balance of Mis12 complex assembly and turnover is required for the efficient and accurate assembly of kinetochore-microtubule binding sites. These findings support a novel role for Hsp90-Sgt1 chaperones in ensuring the fidelity of multiprotein complex assembly.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
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/DSN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/HSP90 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MIS12 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SKP Cullin F-Box Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/SUGT1 protein, human
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
1540-8140
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
19
|
|
pubmed:volume |
189
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
261-74
|
|
pubmed:dateRevised |
2010-10-21
|
|
pubmed:meshHeading |
pubmed-meshheading:20404110-Binding Sites,
pubmed-meshheading:20404110-Cell Cycle Proteins,
pubmed-meshheading:20404110-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:20404110-HSP90 Heat-Shock Proteins,
pubmed-meshheading:20404110-HeLa Cells,
pubmed-meshheading:20404110-Humans,
pubmed-meshheading:20404110-Kinetochores,
pubmed-meshheading:20404110-Microtubule-Associated Proteins,
pubmed-meshheading:20404110-Microtubules,
pubmed-meshheading:20404110-Multiprotein Complexes,
pubmed-meshheading:20404110-Protein Binding,
pubmed-meshheading:20404110-RNA, Small Interfering,
pubmed-meshheading:20404110-Recombinant Fusion Proteins,
pubmed-meshheading:20404110-SKP Cullin F-Box Protein Ligases
|
|
pubmed:year |
2010
|
|
pubmed:articleTitle |
Hsp90-Sgt1 and Skp1 target human Mis12 complexes to ensure efficient formation of kinetochore-microtubule binding sites.
|
|
pubmed:affiliation |
The Section of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|
