Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1998-7-14
pubmed:abstractText
Tyrosine phosphorylation exerts a pivotal role in cell regulation processes of higher eukaryotes. Tight control of the activity of protein tyrosine kinases is crucial for ordered phosphorylation to occur. We have developed a functional screen for tyrosine kinase regulators using c-Src, the first cellular protein tyrosine kinase described, as a prototype; and fission yeast, Schizosaccharomyces pombe, as a genetically amenable host system. Inducible expression of c-Src in fission yeast is lethal. We have screened human cDNA libraries for clones able to counteract the lethal effect of Src. Two different classes of cDNAs, which we called SAS for sequences antagonizing Src, were obtained. The first class encodes for the protein tyrosine kinase Csk, known to regulate Src activity through phosphorylation of the C-terminal tyrosine. The second class consists of clones encoding three different tyrosine phosphatases, counteracting Src action by dephosphorylation of Src substrates and by dephosphorylation of Src itself. The system described here can be applied to identify regulators of other heterologous tyrosine kinases, including receptor-type tyrosine kinases, which impair growth of S. pombe.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1087-0156
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
600-5
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
A functional screen in yeast for regulators and antagonizers of heterologous protein tyrosine kinases.
pubmed:affiliation
European Molecular Biology Laboratory, Heidelberg, Germany. superti@embl-heidelberg.de
pubmed:publicationType
Journal Article, In Vitro