A high phosphorylation state and increased activity of the TRE motif in the NIH3T3 cell transformant induced by retTPC

Yukihito Ishizaka, Masahide Takahashi, Toshikazu Ushijima, Takashi Sugimura, Minako Nagao

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

A 57 kDa protein was detected in an NIH3T3 transformant induced by retTPC, an activated form of the ret proto-oncogene which encodes a receptor-tyrosine kinase. A high phosphorylation state and increased activity of a TPA responsive element was observed in the transformant. Increased expression of c-jun mRNA was also detected. A 40 kDa protein in the retTPC transformant, which was specifically immunoprecipitable with v-jun antiserum, was highly phosphorylated mainly at a serine residue(s). These data suggest that an aberrant signal triggered by a retTPC product affects the cellular serine/threonine phosphorylation state resulting in high phosphorylation of c-jun protein.

Original languageEnglish
Pages (from-to)1331-1336
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume179
Issue number3
DOIs
Publication statusPublished - 30-09-1991
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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