Literature DB >> 1696179

Association between the PDGF receptor and members of the src family of tyrosine kinases.

R M Kypta1, Y Goldberg, E T Ulug, S A Courtneidge.   

Abstract

We have examined the interaction between the platelet-derived growth factor (PDGF) receptor and three src family tyrosine kinases, pp60c-src, p59fyn, and pp62c-yes. The kinase activities of all three enzymes were elevated after PDGF stimulation of quiescent fibroblasts, coincident with association of the src family kinases with the PDGF receptor and other proteins. The presence of a protein of 81-85 kd in these complexes correlated with the detection of phosphatidylinositol (PI) kinase activity (previously described to associate with both the PDGF receptor and pp60c-src-middle T antigen). These results suggest that the physiological response to PDGF involves interaction of the receptor not only with serine/threonine and lipid kinases and a phospholipase, but also with other tyrosine kinases.

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Year:  1990        PMID： 1696179     DOI： 10.1016/0092-8674(90)90013-5

Source DB:  PubMed          Journal:  Cell        ISSN： 0092-8674            Impact factor:   41.582


  170 in total

1.  Src family kinases are required for integrin but not PDGFR signal transduction.

Authors:  R A Klinghoffer; C Sachsenmaier; J A Cooper; P Soriano
Journal:  EMBO J       Date:  1999-05-04       Impact factor: 11.598

2.  Transformation of chicken embryo fibroblasts by v-src uncouples beta1 integrin-mediated outside-in but not inside-out signaling.

Authors:  A Datta; Q Shi; D E Boettiger
Journal:  Mol Cell Biol       Date:  2001-11       Impact factor: 4.272

3.  Purification and characterization of a phosphatidylinositol 3-kinase complex from bovine brain by using phosphopeptide affinity columns.

Authors:  M J Fry; G Panayotou; R Dhand; F Ruiz-Larrea; I Gout; O Nguyen; S A Courtneidge; M D Waterfield
Journal:  Biochem J       Date:  1992-12-01       Impact factor: 3.857

4.  Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences.

Authors:  R J Matthews; D B Bowne; E Flores; M L Thomas
Journal:  Mol Cell Biol       Date:  1992-05       Impact factor: 4.272

5.  SH2 domains of the p85 alpha subunit of phosphatidylinositol 3-kinase regulate binding to growth factor receptors.

Authors:  C J McGlade; C Ellis; M Reedijk; D Anderson; G Mbamalu; A D Reith; G Panayotou; P End; A Bernstein; A Kazlauskas
Journal:  Mol Cell Biol       Date:  1992-03       Impact factor: 4.272

6.  Stable association between the bovine papillomavirus E5 transforming protein and activated platelet-derived growth factor receptor in transformed mouse cells.

Authors:  L Petti; D DiMaio
Journal:  Proc Natl Acad Sci U S A       Date:  1992-08-01       Impact factor: 11.205

7.  An Epstein-Barr virus transformation-associated membrane protein interacts with src family tyrosine kinases.

Authors:  A L Burkhardt; J B Bolen; E Kieff; R Longnecker
Journal:  J Virol       Date:  1992-08       Impact factor: 5.103

8.  eps15, a novel tyrosine kinase substrate, exhibits transforming activity.

Authors:  F Fazioli; L Minichiello; B Matoskova; W T Wong; P P Di Fiore
Journal:  Mol Cell Biol       Date:  1993-09       Impact factor: 4.272

9.  The sites of phosphorylation by protein kinase C and an intact SH2 domain are required for the enhanced response to beta-adrenergic agonists in cells overexpressing c-src.

Authors:  J S Moyers; A H Bouton; S J Parsons
Journal:  Mol Cell Biol       Date:  1993-04       Impact factor: 4.272

10.  The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp.

Authors:  A Kazlauskas; G S Feng; T Pawson; M Valius
Journal:  Proc Natl Acad Sci U S A       Date:  1993-08-01       Impact factor: 11.205
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