Literature DB >> 3103926

Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src.

H Piwnica-Worms, K B Saunders, T M Roberts, A E Smith, S H Cheng.   

Abstract

To investigate the importance of tyrosine phosphorylation in the regulation of pp60c-src, we have substituted phenylalanine for tyrosine at positions 416, 519, and 527. Cells expressing the 527 or the 519/527 mutant but not the 416 or the 519 mutant were morphologically transformed, grew in soft agar, and formed foci. In addition, the 527 and 519/527 mutants had elevated kinase activities in vitro. Modifying Tyr 416 to phenylalanine in the 527 or the 519/527 mutants only partially inhibited their kinase activities yet abolished their ability to induce focus formation and promote growth in soft agar. These results suggest that two events must occur to activate the full transforming potential of pp60c-src: hypophosphorylation at Tyr 527 and hyperphosphorylation at Tyr 416.

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Year:  1987        PMID： 3103926     DOI： 10.1016/0092-8674(87)90757-4

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


  204 in total

1.  Ubiquitin-mediated degradation of active Src tyrosine kinase.

Authors:  K F Harris; I Shoji; E M Cooper; S Kumar; H Oda; P M Howley
Journal:  Proc Natl Acad Sci U S A       Date:  1999-11-23       Impact factor: 11.205

2.  Bruton's tyrosine kinase activity is negatively regulated by Sab, the Btk-SH3 domain-binding protein.

Authors:  T Yamadori; Y Baba; M Matsushita; S Hashimoto; M Kurosaki; T Kurosaki; T Kishimoto; S Tsukada
Journal:  Proc Natl Acad Sci U S A       Date:  1999-05-25       Impact factor: 11.205

3.  Two distinct phosphorylation pathways have additive effects on Abl family kinase activation.

Authors:  Keith Q Tanis; Darren Veach; Henry S Duewel; William G Bornmann; Anthony J Koleske
Journal:  Mol Cell Biol       Date:  2003-06       Impact factor: 4.272

4.  Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo.

Authors:  B J Mayer; P K Jackson; R A Van Etten; D Baltimore
Journal:  Mol Cell Biol       Date:  1992-02       Impact factor: 4.272

5.  The only domain which distinguishes Epstein-Barr virus latent membrane protein 2A (LMP2A) from LMP2B is dispensable for lymphocyte infection and growth transformation in vitro; LMP2A is therefore nonessential.

Authors:  R Longnecker; C L Miller; X Q Miao; A Marchini; E Kieff
Journal:  J Virol       Date:  1992-11       Impact factor: 5.103

6.  Tyrosine phosphorylation of a c-Src-like protein is increased in membranes of CD4- CD8- T lymphocytes from lpr/lpr mice.

Authors:  T Katagiri; J P Ting; R Dy; C Prokop; P Cohen; H S Earp
Journal:  Mol Cell Biol       Date:  1989-11       Impact factor: 4.272

7.  En bloc substitution of the Src homology region 2 domain activates the transforming potential of the c-Abl protein tyrosine kinase.

Authors:  A J Muller; A M Pendergast; K Parmar; M H Havlik; N Rosenberg; O N Witte
Journal:  Proc Natl Acad Sci U S A       Date:  1993-04-15       Impact factor: 11.205

8.  Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae.

Authors:  S M Murphy; M Bergman; D O Morgan
Journal:  Mol Cell Biol       Date:  1993-09       Impact factor: 4.272

9.  Myristylation is required for Tyr-527 dephosphorylation and activation of pp60c-src in mitosis.

Authors:  S Bagrodia; S J Taylor; D Shalloway
Journal:  Mol Cell Biol       Date:  1993-03       Impact factor: 4.272

10.  Kinetics of p56lck and p60src Src homology 2 domain binding to tyrosine-phosphorylated peptides determined by a competition assay or surface plasmon resonance.

Authors:  G Payne; S E Shoelson; G D Gish; T Pawson; C T Walsh
Journal:  Proc Natl Acad Sci U S A       Date:  1993-06-01       Impact factor: 11.205
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