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

doi:10.1016/0014-5793(92)80353-I

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 journal › Article › peer-review

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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 K_m and V_max 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 language	English
Pages (from-to)	171-174
Number of pages	4
Journal	FEBS Letters
Volume	297
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(92)80353-I
Publication status	Published - 03-02-1992
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(92)80353-I

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title = "Phosphorylation of smg p21B/rap1B p21 by cyclic GMP-dependent protein kinase",

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.",

author = "Yasushi Miura and Kozo Kaibuchi and Takahito Itoh and Corbin, {Jackie D.} and Francis, {Sharron H.} and Yoshimi Takai",

note = "Funding Information: nclrrro~rtlr~~scrt~cr,rs: This investigation at Kobc University was supported by grants-in-aid for Scientific Research and Cancer Research from the Ministry of Education, Science and Culture. Japan (1991), a grant-in-aid for Abnormalities in Hormone Receptor Mechanisms from the Ministry of Health and Welfare, Japan (1991). and by grants from the Human Front& Science Program (199l), the Yamanouchi Foundation for Research on Metabolic Disease (1991). and the Research Program on Cell Calcium Signal in the Cardiovascular Srstcm (1991). Janan. This invcstination at Vanderbilt University Las supported bi NIH DK40029.-We arc grateful to J. Yamaguchi for her sccretariul assistance.",

year = "1992",

month = feb,

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doi = "10.1016/0014-5793(92)80353-I",

language = "English",

volume = "297",

pages = "171--174",

journal = "FEBS Letters",

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TY - JOUR

T1 - Phosphorylation of smg p21B/rap1B p21 by cyclic GMP-dependent protein kinase

AU - Miura, Yasushi

AU - Kaibuchi, Kozo

AU - Itoh, Takahito

AU - Corbin, Jackie D.

AU - Francis, Sharron H.

AU - Takai, Yoshimi

N1 - Funding Information: nclrrro~rtlr~~scrt~cr,rs: This investigation at Kobc University was supported by grants-in-aid for Scientific Research and Cancer Research from the Ministry of Education, Science and Culture. Japan (1991), a grant-in-aid for Abnormalities in Hormone Receptor Mechanisms from the Ministry of Health and Welfare, Japan (1991). and by grants from the Human Front& Science Program (199l), the Yamanouchi Foundation for Research on Metabolic Disease (1991). and the Research Program on Cell Calcium Signal in the Cardiovascular Srstcm (1991). Janan. This invcstination at Vanderbilt University Las supported bi NIH DK40029.-We arc grateful to J. Yamaguchi for her sccretariul assistance.

PY - 1992/2/3

Y1 - 1992/2/3

N2 - 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.

AB - 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.

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DO - 10.1016/0014-5793(92)80353-I

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

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