Linked Life Data

1312697

Source:http://linkedlifedata.com/resource/pubmed/id/1312697

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-4-20
pubmed:abstractText
The L-myc protein migrates as three distinct differentially phosphorylated bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). This phosphorylation can be rapidly increased either by treatment with the protein kinase C (PKC) activator phorbol ester 12-O-tetradecanoyl-phorbol-13-acetate (TPA) or by inhibition of serine/threonine protein phosphatases with okadaic acid. In vitro mutagenesis and phosphoamino acid analyses define the N-terminal serine residues 38 and 42 of L-myc as critical targets for the PKC-dependent phosphorylation. These are the exclusive sites of phosphorylation in the N-terminal third of the L-myc protein, and can be phosphorylated in vitro by glycogen synthase kinase 3 beta (GSK-3 beta). A mutant L-myc protein in which these serines have been replaced by alanine residues does not show heterogeneous electrophoretic migration or hyperphosphorylation in response to PKC activation, and is not a substrate for GSK-3 beta in vitro. Similar potential phosphorylation sites are present in c-myc and N-myc in a highly conserved region thought to represent a transcriptional activation domain. We suggest that N-terminal phosphorylation of the L-myc protein is a means of rapid regulation of this oncoprotein, possibly mediated in vivo by the action of GSK-3.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:geneSymbol
L-myc
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
347-53
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:1312697-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:1312697-Cell Cycle, pubmed-meshheading:1312697-Cells, Cultured, pubmed-meshheading:1312697-DNA Mutational Analysis, pubmed-meshheading:1312697-Ethers, Cyclic, pubmed-meshheading:1312697-Glycogen Synthase Kinases, pubmed-meshheading:1312697-Humans, pubmed-meshheading:1312697-Okadaic Acid, pubmed-meshheading:1312697-Phosphoprotein Phosphatases, pubmed-meshheading:1312697-Phosphoproteins, pubmed-meshheading:1312697-Phosphorylation, pubmed-meshheading:1312697-Phosphoserine, pubmed-meshheading:1312697-Polymerase Chain Reaction, pubmed-meshheading:1312697-Protein Kinase C, pubmed-meshheading:1312697-Protein Kinases, pubmed-meshheading:1312697-Proto-Oncogene Proteins c-myc, pubmed-meshheading:1312697-Structure-Activity Relationship, pubmed-meshheading:1312697-Trans-Activators
pubmed:year
1992
pubmed:articleTitle
Activation of protein kinase C increases phosphorylation of the L-myc trans-activator domain at a GSK-3 target site.
pubmed:affiliation
Department of Virology, University of Helsinki, Finland.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't