rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2006-9-11
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pubmed:abstractText |
Polo-like kinase functions are essential for the establishment of a normal bipolar mitotic spindle, although precisely how Plk1 regulates the spindle is uncertain. In this study, we report that the small GTP/GDP-binding protein Ran is associated with Plk1. Plk1 is capable of phosphorylating co-immunoprecipitated Ran in vitro on serine-135 and Ran is phosphorylated in vivo at the same site during mitosis when Plk1 is normally activated. Cell cultures over-expressing a Ran S135D mutant have significantly higher numbers of abnormal mitotic cells than those over-expressing either wild-type or S135A Ran. The abnormalities in S135D mutant cells are similar to cells over-expressing Plk1. Our data suggests that Ran is a physiological substrate of Plk1 and that Plk1 regulates the spindle organization partially through its phosphorylation on Ran.
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pubmed:grant |
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0006-291X
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pubmed:author |
pubmed-author:ConradsThomas PTP,
pubmed-author:CopelandTerry DTD,
pubmed-author:DimitrovDimiter SDS,
pubmed-author:FerrisAndreaA,
pubmed-author:FerrisDouglass KDK,
pubmed-author:FisherRebeccaR,
pubmed-author:HughesSteveS,
pubmed-author:LongoDan LDL,
pubmed-author:MaloidSharon CSC,
pubmed-author:VeenstraTimothy DTD,
pubmed-author:YangFengF,
pubmed-author:YuanJin HuiJH
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pubmed:issnType |
Print
|
pubmed:day |
13
|
pubmed:volume |
349
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
144-52
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:16930555-Animals,
pubmed-meshheading:16930555-Binding Sites,
pubmed-meshheading:16930555-Cell Cycle Proteins,
pubmed-meshheading:16930555-Cell Line,
pubmed-meshheading:16930555-Cell Line, Tumor,
pubmed-meshheading:16930555-Dogs,
pubmed-meshheading:16930555-Guanosine Triphosphate,
pubmed-meshheading:16930555-Humans,
pubmed-meshheading:16930555-Mitosis,
pubmed-meshheading:16930555-Mutation,
pubmed-meshheading:16930555-Phosphorylation,
pubmed-meshheading:16930555-Protein Binding,
pubmed-meshheading:16930555-Protein-Serine-Threonine Kinases,
pubmed-meshheading:16930555-Proto-Oncogene Proteins,
pubmed-meshheading:16930555-Serine,
pubmed-meshheading:16930555-ran GTP-Binding Protein
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pubmed:year |
2006
|
pubmed:articleTitle |
Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation.
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pubmed:affiliation |
Laboratory of Cancer Prevention, NCI at Frederick, Frederick, MD, USA; Nanobiology Program, CCR, NCI at Frederick, Frederick, MD, USA. yfeng@mail.ncifcrf.gov
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
|