Linked Life Data

15344887

Source:http://linkedlifedata.com/resource/pubmed/id/15344887

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2004-9-3
pubmed:abstractText
Cdc25A phosphatase regulates cell cycle progression by removing the inhibitory phosphates from cyclin-dependent kinases. Activity of Cdc25A depends on its phosphorylation status. During normal cell cycle progression and after DNA damage phosphorylation by Chk1 (or Chk2) triggers Cdc25A degradation via ubiquitin-proteasome pathway. In this study we investigate the role of various phosphorylation sites (Ser123, Ser75, Ser17 and Ser115) in the regulation of Cdc25A stability. We have shown that only S75A mutation abrogates Cdc25A degradation both in normal and stress conditions. We also studied the influence of stable form of Cdc25A on checkpoint progression after DNA damage. We have found out that delay in DNA synthesis after UV and IR does not depend on Cdc25A activity. However, the presence of stable Cdc25A increases the number of mitotic cells after these stresses.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0041-3771
pubmed:author
pubmed:issnType
Print
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
423-30
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
[Degradation of Cdc25A phosphatase in HeLa cells under normal and stress conditions].
pubmed:publicationType
Journal Article, Comparative Study, English Abstract, Research Support, Non-U.S. Gov't