A protein histidine kinase induced m rat liver by peroxisome proliferators. In vitro activation by Ras protein and guanine nucleotides

Kiyoto Motojima, S. Goto

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

A novel protein kinase is induced in rat liver plasma membrane by the administration of peroxisome proliferators. A 36 kDa protein (P36) on the membrane was rapidly phosphorylated in vitro by the kinase and the phosphorylated amino acid was identified as phosphohistidine. Histidine phosphorylation of P36 was activated in vitro by recombinant Ras protein and GTP; both decreased Michaelis constant (Km) for ATP from 1.25 to 0.25 μM. The novel histidine kinase, products of which have been overlooked due to their acid lability, may participate in cellular signaling and peroxisome proliferators may perturb the pathway.

Original languageEnglish
Pages (from-to)75-79
Number of pages5
JournalFEBS Letters
Volume319
Issue number1-2
DOIs
Publication statusPublished - Mar 15 1993

Fingerprint

Peroxisome Proliferators
ras Proteins
Guanine Nucleotides
Histidine
Liver
Rats
Phosphotransferases
Chemical activation
Cell signaling
Recombinant proteins
Phosphorylation
Cell membranes
Guanosine Triphosphate
Recombinant Proteins
Protein Kinases
Proteins
Adenosine Triphosphate
Cell Membrane
Membranes
Amino Acids

Keywords

  • Histidine kinase
  • Peroxisome proliferator
  • Ras protein
  • Rat liver
  • Signal transduction

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A protein histidine kinase induced m rat liver by peroxisome proliferators. In vitro activation by Ras protein and guanine nucleotides. / Motojima, Kiyoto; Goto, S.

In: FEBS Letters, Vol. 319, No. 1-2, 15.03.1993, p. 75-79.

Research output: Contribution to journalArticle

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