Phosphorylation of smg p21B/rap1B p21 by cyclic GMP-dependent protein kinase

Yasushi Miura, Kozo Kaibuchi, Takahito Itoh, Jackie D. Corbin, Sharron H. Francis, Yoshimi Takai

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

smg p21B/rap1B p21, a member of ras p21-like small GTP-binding protein superfamily, has been shown to be phosphorylated by cyclic AMP-dependent protein kinase (protein kinase A). We show here that this protein was also phosphorylated by cyclic GMP-dependent protein kinase (protein kinase G) in a cell-free system. The same serine residue (Ser179) in the C-terminal region was phosphorylated by both protein kinases G and A. The Km and Vmax values of smg p21B for protein kinase G were 5 × 10-7 M and 4 × 10-9 mol/min/mg, and those values for protein kinase A were 1 × 10-7 M and 3 × 10-8 mol/min/mg.

Original languageEnglish
Pages (from-to)171-174
Number of pages4
JournalFEBS Letters
Volume297
Issue number1-2
DOIs
Publication statusPublished - 03-02-1992

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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