Linked Life Data

15380617

Source:http://linkedlifedata.com/resource/pubmed/id/15380617

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2004-9-21
pubmed:abstractText
Chk2 is a key player of the DNA damage signalling pathway. To identify new regulators of this kinase, we performed a yeast two-hybrid screen and found that Chk2 associated with the B' regulatory subunit of protein phosphatase PP2A. In vitro GST-Chk2 pulldowns demonstrated that B'gamma isoforms bound to Chk2 with the strongest apparent affinity. This was confirmed in cellulo by co-immunoprecipitation after overexpression of the respective partners in HEK293 cells. The A and C subunits of PP2A were present in the complexes, suggesting that Chk2 was associated with a functionnal PP2A. In vitro kinase assays showed that B'gamma3 was a potent Chk2 substrate. This phosphorylation increased the catalytic phosphatase activity of PP2A measured on MAP kinase-phosphorylated myelin basic protein as well as on autophosphorylated Chk2. Finally, we demonstrated that overexpressing B'gamma3 in HEK293 suppressed the phosphorylation of Chk2 induced by a genotoxic treatment, suggesting that PP2A may counteract the action of the checkpoint kinase in living cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0248-4900
pubmed:author
pubmed:copyrightInfo
Copyright 2004 Elsevier SAS
pubmed:issnType
Print
pubmed:volume
96
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
509-17
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Regulation of Chk2 phosphorylation by interaction with protein phosphatase 2A via its B' regulatory subunit.
pubmed:affiliation
Laboratoire de Biologie Cellulaire et Moléculaire du Contrôle de la Prolifération, UMR 5088 CNRS, Institut Fédératif de Recherche 109, Université Paul Sabatier, Bât 4R3-B1, 118 route de Narbonne, 31062 Toulouse, France. dozier@cict.fr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't