Linked Life Data

8910336

Source:http://linkedlifedata.com/resource/pubmed/id/8910336

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
44
pubmed:dateCreated
1996-12-26
pubmed:abstractText
The protein-tyrosine kinase Lck is essential for signaling through the T-cell antigen receptor. Treatment of T-cells with a variety of extracellular stimuli increases the phosphorylation of Lck on serine residues. This results in shifts in the apparent molecular weight of Lck to forms that exhibit reduced electrophoretic mobility on SDS-polyacrylamide gels. We found that as a result of arresting cells in mitosis, forms of Lck were generated that migrated with slower mobilities on SDS-polyacrylamide gels. This suggested that a serine/threonine kinase, active at mitosis, was phosphorylating Lck. Using antibodies to Lck and to the cyclin-dependent serine kinase, Cdc2, as well as the cyclin-dependent kinase affinity resin, Suc1-agarose, we detected a stable interaction between Lck and Cdc2. The interaction was mediated through the Src homology 3 domain of Lck and was selective, as only the active form of Cdc2 was found to associate with Lck. Moreover, Cdc2 was able to phosphorylate Lck in vitro and shift its electrophoretic mobility to a more slowly migrating form. An association between active Cdc2 and the Src-related kinases Lyn and Fyn was also demonstrated, although Cdc2 was not found associated with the tyrosine kinases, Csk and Syk. These results demonstrate that at mitosis, Cdc2 associates with and phosphorylates Lck.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27517-23
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
The protein-tyrosine kinase Lck associates with and is phosphorylated by Cdc2.
pubmed:affiliation
Department of Biology, Purdue University, West Lafayette, Indiana 47907, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.