Literature DB >> 6437865

pp60c-src is a substrate for phosphorylation when cells are stimulated to enter cycle.

T Tamura, R R Friis, H Bauer.   

Abstract

The endogenous cellular oncogene products, pp60c-src, exhibits a protein kinase activity, but is itself a phosphoprotein. Based on the assumption that pp60c-src might play a role in the control of cell proliferation, we have studied its behaviour as a substrate for phosphorylation known to occur when quiescent, serum-deprived cells are stimulated to enter cell cycle following addition of either serum, platelet-derived growth factor or the phorbol ester derivative, 12-O-tetradecanoyl-phorbol-13-acetate. For this purpose a partial purification of pp60c-src on DEAE ion-exchange chromatography was combined with immune precipitation. A 2-4-fold increase in serine phosphorylation of pp60c-src was consistently observed after stimulation of quiescent cells to growth.

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Year:  1984        PMID: 6437865     DOI: 10.1016/0014-5793(84)81001-7

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  10 in total

1.  The product of the protooncogene c-src is modified during the cellular response to platelet-derived growth factor.

Authors:  R Ralston; J M Bishop
Journal:  Proc Natl Acad Sci U S A       Date:  1985-12       Impact factor: 11.205

2.  Augmented mitogenic responsiveness to epidermal growth factor in murine fibroblasts that overexpress pp60c-src.

Authors:  D K Luttrell; L M Luttrell; S J Parsons
Journal:  Mol Cell Biol       Date:  1988-01       Impact factor: 4.272

3.  Substitution of Ser-17 of pp60c-src: biological and biochemical characterization in chicken embryo fibroblasts.

Authors:  Y Hirota; J Kato; T Takeya
Journal:  Mol Cell Biol       Date:  1988-04       Impact factor: 4.272

4.  Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity.

Authors:  K L Gould; T Hunter
Journal:  Mol Cell Biol       Date:  1988-08       Impact factor: 4.272

5.  pp60c-src tyrosine kinase, myristylation, and modulatory domains are required for enhanced mitogenic responsiveness to epidermal growth factor seen in cells overexpressing c-src.

Authors:  L K Wilson; D K Luttrell; J T Parsons; S J Parsons
Journal:  Mol Cell Biol       Date:  1989-04       Impact factor: 4.272

6.  Mutation of amino acids in pp60c-src that are phosphorylated by protein kinases C and A.

Authors:  P Yaciuk; J K Choi; D Shalloway
Journal:  Mol Cell Biol       Date:  1989-06       Impact factor: 4.272

7.  Early activation of endogenous pp60src kinase activity during neuronal differentiation of cultured human neuroblastoma cells.

Authors:  C Bjelfman; G Meyerson; C A Cartwright; K Mellström; U Hammerling; S Påhlman
Journal:  Mol Cell Biol       Date:  1990-01       Impact factor: 4.272

8.  gp140v-fms molecules expressed at the surface of cells transformed by the McDonough strain of feline sarcoma virus are phosphorylated in tyrosine and serine.

Authors:  T Tamura; E Simon; H Niemann; G T Snoek; H Bauer
Journal:  Mol Cell Biol       Date:  1986-12       Impact factor: 4.272

9.  Activation of the pp60c-src kinase during differentiation of monomyelocytic cells in vitro.

Authors:  A Barnekow; M Gessler
Journal:  EMBO J       Date:  1986-04       Impact factor: 11.598

10.  Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells.

Authors:  T David-Pfeuty; Y Nouvian-Dooghe
Journal:  J Cell Biol       Date:  1990-12       Impact factor: 10.539

  10 in total

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