Linked Life Data

8058338

Source:http://linkedlifedata.com/resource/pubmed/id/8058338

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1994-9-15
pubmed:abstractText
Cyclin D1 is a nuclear phosphoprotein that is thought to play a major role in the control of G0/G1-->S progression. The fact that its expression is not tightly regulated during cell cycle progression suggests that its activity might be modulated by post-translational mechanisms. In the present study, we show that out of five serine-threonine kinases tested only protein kinase A (PKA) was able to phosphorylate cyclin D1 in vitro. In agreement with this observation, forskolin treatment, but not TPA stimulation, led to increased phosphorylation of cyclin D1 in vivo. Phosphoamino acid analysis and two-dimensional phosphopeptide mapping of wild-type and truncated cyclin D1 proteins showed that PKA phosphorylates three distinct serine residues in cyclin D1 at positions 90, 197 and 234. Serine-90 is located within the cyclin box, raising the possibility that phosphorylation of cyclin D1 might play a role in regulating the interaction with other proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2733-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Protein kinase A phosphorylates cyclin D1 at three distinct sites within the cyclin box and at the C-terminus.
pubmed:affiliation
Institut für Molekularbiologie und Tumorforschung (IMT), Philipps Universität Marburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't