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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2009-1-1
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pubmed:abstractText |
Timely degradation of regulatory proteins by the ubiquitin proteolytic pathway (UPP) is an established paradigm of cell cycle regulation during the G2/M and G1/S transitions. Less is known about roles for the UPP during S phase. Here we present evidence that dynamic cell cycle-dependent changes in levels of UbcH7 regulate entrance into and progression through S phase. In diverse cell lines, UbcH7 protein levels are dramatically reduced in S phase but are fully restored by G2. Knockdown of UbcH7 increases the proportion of cells in S phase and doubles the time to traverse S phase, whereas UbcH7 overexpression reduces the proportion of cells in S phase. These data suggest a role for UbcH7 targets in the completion of S phase and entry into G2. Notably, UbcH7 knockdown was coincident with elevated levels of the checkpoint kinase Chk1 but not Chk2. These results argue that UbcH7 promotes S phase progression to G2 by modulating the intra-S phase checkpoint mediated by Chk1. Furthermore, UbcH7 levels appear to be regulated by a UPP. Together the data identify novel roles for the UPP, specifically UbcH7 in the regulation of S phase transit time as well as in cell proliferation.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-10375532,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-10531381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-10558980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-10559916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-10564281,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-10859164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-10888878,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-10966114,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-11035045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-11072070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-11141301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-11241344,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-11846513,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-12620973,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-12628165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-12676583,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-12853964,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-17218260,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-18562292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-8901595,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-9688277,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/18946090-9990509
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Checkpoint kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/PTEN Phosphohydrolase,
http://linkedlifedata.com/resource/pubmed/chemical/PTEN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/UBE2L3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Conjugating Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/checkpoint kinase 2
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1939-4586
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-9
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:18946090-Animals,
pubmed-meshheading:18946090-Cell Cycle,
pubmed-meshheading:18946090-Cell Line,
pubmed-meshheading:18946090-Gene Knockdown Techniques,
pubmed-meshheading:18946090-Humans,
pubmed-meshheading:18946090-PTEN Phosphohydrolase,
pubmed-meshheading:18946090-Proteasome Endopeptidase Complex,
pubmed-meshheading:18946090-Protein Kinases,
pubmed-meshheading:18946090-Protein-Serine-Threonine Kinases,
pubmed-meshheading:18946090-S Phase,
pubmed-meshheading:18946090-Ubiquitin,
pubmed-meshheading:18946090-Ubiquitin-Conjugating Enzymes
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pubmed:year |
2009
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pubmed:articleTitle |
Novel control of S phase of the cell cycle by ubiquitin-conjugating enzyme H7.
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pubmed:affiliation |
Jean Mayer USDA Human Nutrition Research Center on Aging, Tufts University, Boston, MA 02111, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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