Linked Life Data

8195176

Source:http://linkedlifedata.com/resource/pubmed/id/8195176

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1994-6-29
pubmed:abstractText
The phosphorylation of proteins at tyrosine residues is critical in cellular signal transduction and neoplastic transformation. These mechanisms are regulated by the activities of both protein-tyrosine kinases and protein-tyrosine phosphatases. Recent studies have identified a novel protein-tyrosine phosphatase, termed Syp, that is widely expressed in various tissues. Syp encodes a cytoplasmic phosphatase that contains two Src homology 2 (SH2) domains. Since SH2 domains have been shown to target the association of signal-transducing molecules to activated tyrosine kinases, experiments were performed to determine whether Syp might form specific complexes with p210bcr-abl, a fusion protein believed to be involved in the pathogenesis of chronic myelogenous leukemia and, thus, possibly alter or mediate p210bcr-abl tyrosine kinase activity. We found that Syp was highly and constitutively tyrosine phosphorylated in three different murine cell lines transfected with a p210bcr-abl expression vector. Furthermore, p210bcr-abl, Syp, and Grb2 formed stable complexes in BCR-ABL-expressing cells. Complex formation between p210bcr-abl and Syp was mediated in vitro by the NH2-terminal SH2 domain of Syp. Last, p210bcr-abl tyrosine kinase was effectively dephosphorylated by Syp in vitro. These results suggest an interaction between Syp and BCR-ABL protein, which might play a role in cellular transformation of BCR-ABL.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15381-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8195176-Animals, pubmed-meshheading:8195176-Cell Line, pubmed-meshheading:8195176-Fusion Proteins, bcr-abl, pubmed-meshheading:8195176-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:8195176-Mice, pubmed-meshheading:8195176-Phosphorylation, pubmed-meshheading:8195176-Precipitin Tests, pubmed-meshheading:8195176-Protein Tyrosine Phosphatase, Non-Receptor Type 11, pubmed-meshheading:8195176-Protein Tyrosine Phosphatase, Non-Receptor Type 6, pubmed-meshheading:8195176-Protein Tyrosine Phosphatases, pubmed-meshheading:8195176-Protein-Tyrosine Kinases, pubmed-meshheading:8195176-SH2 Domain-Containing Protein Tyrosine Phosphatases, pubmed-meshheading:8195176-Signal Transduction, pubmed-meshheading:8195176-Substrate Specificity, pubmed-meshheading:8195176-Transfection
pubmed:year
1994
pubmed:articleTitle
SH2-containing phosphotyrosine phosphatase Syp is a target of p210bcr-abl tyrosine kinase.
pubmed:affiliation
Department of Medicine (Hematology/Oncology), Indiana University School of Medicine, Indianapolis 46202.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.