Linked Life Data

1372400

Source:http://linkedlifedata.com/resource/pubmed/id/1372400

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-4-20
pubmed:abstractText
Members of the src family of tyrosine kinases are composed of amino acid sequences which can be divided into three regions: the unique amino-terminal 80 residues; the next 180 residues of conserved but non-catalytic sequence; and the catalytic carboxy-terminal half of the molecule. To characterize the elements that regulate the catalytic and transforming activities of two members of this family, pp59c-fyn and pp60c-src, we generated six chimeric proteins by interchanging the three regions of the 531F mutant of pp59c-fyn and of the 527F mutant of pp60c-src. Our data indicate that substituting all or part of the amino-terminal 263 residues of pp59c-fyn for those of 527F inhibited the kinase and transforming activities of 527F. Conversely, substituting the amino-terminal half of pp60c-src for that of 531F resulted in an increase in the transforming potential of 531F. These results suggest that the amino-terminal half of pp59c-fyn contains elements which act to suppress the catalytic and transforming activities of the enzyme and that these suppressive elements are either absent or inactive in pp60c-src. These differences argue that the src family of tyrosine kinases are regulated differently in the cell. In vitro translation of some of the chimeras in rabbit reticulocyte lysates generated a 75 kDa protein in addition to the expected 59 kDa product. This 75 kDa species is analogous to the p75 protein previously detected in wild-type pp59c-fyn translation products. Interestingly, formation of p75 required the presence of DNA sequences encoding the unique amino-terminal residues of pp59c-fyn.
pubmed:grant
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
c-src
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
317-22
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:1372400-Animals, pubmed-meshheading:1372400-Base Sequence, pubmed-meshheading:1372400-Cell Transformation, Neoplastic, pubmed-meshheading:1372400-Chickens, pubmed-meshheading:1372400-Humans, pubmed-meshheading:1372400-Molecular Sequence Data, pubmed-meshheading:1372400-Molecular Weight, pubmed-meshheading:1372400-Mutagenesis, Site-Directed, pubmed-meshheading:1372400-Oligodeoxyribonucleotides, pubmed-meshheading:1372400-Peptide Mapping, pubmed-meshheading:1372400-Protein-Tyrosine Kinases, pubmed-meshheading:1372400-Proto-Oncogene Proteins, pubmed-meshheading:1372400-Proto-Oncogene Proteins c-fyn, pubmed-meshheading:1372400-Proto-Oncogene Proteins pp60(c-src), pubmed-meshheading:1372400-Recombinant Fusion Proteins, pubmed-meshheading:1372400-Structure-Activity Relationship
pubmed:year
1992
pubmed:articleTitle
The amino-terminal half of pp59c-fyn contains sequences necessary for formation of a 75 kDa form and also repressive elements absent in pp60c-src.
pubmed:affiliation
Laboratory of Cellular Regulation, Genzyme Corporation, Framingham, Massachusetts 01701.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.