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Enzymatically inactive p60c-src mutant with altered ATP-binding site is fully phosphorylated in its carboxy-terminal regulatory region.

Publication ,  Journal Article
Jove, R; Kornbluth, S; Hanafusa, H
Published in: Cell
September 1987

Cellular src protein, p60c-src, is phosphorylated on tyrosine 527 in chicken embryo fibroblasts, and this phosphorylation is implicated in suppressing the protein-tyrosine kinase activity and transforming potential of p60c-src. To determine whether tyrosine 527 phosphorylation is dependent on p60c-src kinase activity, the ATP-binding site of chicken p60c-src was destroyed by substitution of lysine 295 with methionine. The resultant protein, p60c-src(M295), expressed either in chicken cells or in yeast, lacked detectable kinase activity. Nevertheless, tyrosine and serine phosphorylation of p60c-src(M295) overproduced in chicken cells were indistinguishable from that of authentic p60c-src. By contrast, p60c-src(M295) was not phosphorylated on tyrosine in yeast. These results suggest that a protein kinase present in chicken cells but not in yeast phosphorylates tyrosine 527 in trans, and are consistent with the possibility that this kinase is distinct from p60c-src.

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Published In

Cell

DOI

EISSN

1097-4172

ISSN

0092-8674

Publication Date

September 1987

Volume

50

Issue

6

Start / End Page

937 / 943

Related Subject Headings

  • Tyrosine
  • Saccharomyces cerevisiae
  • Recombinant Proteins
  • Proto-Oncogene Proteins pp60(c-src)
  • Proto-Oncogene Proteins
  • Protein-Tyrosine Kinases
  • Protein Kinases
  • Phosphotyrosine
  • Phosphorylation
  • Fibroblasts
 

Citation

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Jove, R., Kornbluth, S., & Hanafusa, H. (1987). Enzymatically inactive p60c-src mutant with altered ATP-binding site is fully phosphorylated in its carboxy-terminal regulatory region. Cell, 50(6), 937–943. https://doi.org/10.1016/0092-8674(87)90520-4
Jove, R., S. Kornbluth, and H. Hanafusa. “Enzymatically inactive p60c-src mutant with altered ATP-binding site is fully phosphorylated in its carboxy-terminal regulatory region.Cell 50, no. 6 (September 1987): 937–43. https://doi.org/10.1016/0092-8674(87)90520-4.
Jove, R., et al. “Enzymatically inactive p60c-src mutant with altered ATP-binding site is fully phosphorylated in its carboxy-terminal regulatory region.Cell, vol. 50, no. 6, Sept. 1987, pp. 937–43. Epmc, doi:10.1016/0092-8674(87)90520-4.
Journal cover image

Published In

Cell

DOI

EISSN

1097-4172

ISSN

0092-8674

Publication Date

September 1987

Volume

50

Issue

6

Start / End Page

937 / 943

Related Subject Headings

  • Tyrosine
  • Saccharomyces cerevisiae
  • Recombinant Proteins
  • Proto-Oncogene Proteins pp60(c-src)
  • Proto-Oncogene Proteins
  • Protein-Tyrosine Kinases
  • Protein Kinases
  • Phosphotyrosine
  • Phosphorylation
  • Fibroblasts