Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2008-6-2
pubmed:abstractText
The cell division control protein 6 (Cdc6) is essential for formation of pre-replication complexes at origins of DNA replication. Phosphorylation of Cdc6 by cyclin-dependent kinases inhibits ubiquitination of Cdc6 by APC/C(cdh1) and degradation by the proteasome. Experiments described here show that the PR70 member of the PPP2R3 family of regulatory subunits targets protein phosphatase 2A (PP2A) to Cdc6. Interaction with Cdc6 is mediated by residues within the C terminus of PR70, whereas interaction with PP2A requires N-terminal sequences conserved within the PPP2R3 family. Two functional EF-hand calcium-binding motifs mediate a calcium-enhanced interaction of PR70 with PP2A. Calcium has no effect on the interaction of PR70 with Cdc6 but enhances the association of PP2A with Cdc6 through its effects on PR70. Knockdown of PR70 by RNA interference results in an accumulation of endogenous and expressed Cdc6 protein that is dependent on the cyclin-dependent protein kinase phosphorylation sites on Cdc6. Knockdown of PR70 also causes G(1) arrest, suggesting that PR70 function is critical for progression into S phase. These observations indicate that PP2A can be targeted in a calcium-regulated manner to Cdc6 via the PR70 subunit, where it plays a role in regulating protein phosphorylation and stability.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-10339564, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-10629059, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-10712915, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-10806104, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-10929717, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-10995389, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-11018019, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-11046155, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-11102512, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-11171037, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-11346650, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-11856313, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-11904383, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-11929880, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-11997504, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-12045100, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-12208841, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-12372823, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-12524438, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-12605688, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-14749377, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-14871926, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-15380092, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-15687260, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-16055707, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-16153703, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-16567647, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-16581779, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-17535922, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-2673026, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-2997181, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-6715311, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-8252625, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-8990175, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-9520412, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-9889196, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-9927208, http://linkedlifedata.com/resource/pubmed/commentcorrection/18397887-9989501
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
283
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16104-14
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:18397887-Amino Acid Motifs, pubmed-meshheading:18397887-Animals, pubmed-meshheading:18397887-COS Cells, pubmed-meshheading:18397887-Cadherins, pubmed-meshheading:18397887-Calcium, pubmed-meshheading:18397887-Cell Cycle Proteins, pubmed-meshheading:18397887-Cercopithecus aethiops, pubmed-meshheading:18397887-DNA Replication, pubmed-meshheading:18397887-G1 Phase, pubmed-meshheading:18397887-HeLa Cells, pubmed-meshheading:18397887-Humans, pubmed-meshheading:18397887-Nuclear Proteins, pubmed-meshheading:18397887-Phosphorylation, pubmed-meshheading:18397887-Proteasome Endopeptidase Complex, pubmed-meshheading:18397887-Protein Phosphatase 2, pubmed-meshheading:18397887-Protein Subunits, pubmed-meshheading:18397887-Replication Origin, pubmed-meshheading:18397887-S Phase, pubmed-meshheading:18397887-Ubiquitination
pubmed:year
2008
pubmed:articleTitle
Protein phosphatase 2A is targeted to cell division control protein 6 by a calcium-binding regulatory subunit.
pubmed:affiliation
Department of Pharmacology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-9041, USA.
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