Both stimulatory and inhibitory GDP GTP exchange proteins, smg GDS and rho GDI, are active on multiple small GTP-binding proteins

Kunihiko Hiraoka; Kozo Kaibuchi; Satoshi Ando; Takashi Musha; Kenji Takaishi; Takakazu Mizuno; Makoto Asada; Luc Ménard; Eric Tomhave; John Didsbury; Ralph Snyderman; Yoshimi Takai

doi:10.1016/0006-291X(92)91820-G

Both stimulatory and inhibitory GDP GTP exchange proteins, smg GDS and rho GDI, are active on multiple small GTP-binding proteins

Kunihiko Hiraoka, Kozo Kaibuchi, Satoshi Ando, Takashi Musha, Kenji Takaishi, Takakazu Mizuno, Makoto Asada, Luc Ménard, Eric Tomhave, John Didsbury, Ralph Snyderman, Yoshimi Takai

Research output: Contribution to journal › Article › peer-review

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Abstract

Six peaks of small GTP-binding proteins (G proteins) were separated by column chromatographies from the cytosol fraction of the differentiated HL-60 cells: two peaks of rho p21, one peak of smg rap1 p21, two peaks of rac1 p21, and one peak of an unidentified small G protein with a Mr of about 20,000 (20 KG). smg GDS, previously thought to be a stimulatory GDP GTP exchange protein for smg p21, Ki-ras p21, and rho p21, but not for Ha-ras p21 or smg p25A, was also active on rac1 p21. rho GDI, previously thought to be an inhibitory GDP GTP exchange protein specific for rho p21, was also active on rac1 p21. These results indicate that both smg GDS and rho GDI are active on multiple small G proteins.

Original language	English
Pages (from-to)	921-930
Number of pages	10
Journal	Biochemical and Biophysical Research Communications
Volume	182
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(92)91820-G
Publication status	Published - 31-01-1992
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(92)91820-G

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Hiraoka, K., Kaibuchi, K., Ando, S., Musha, T., Takaishi, K., Mizuno, T., Asada, M., Ménard, L., Tomhave, E., Didsbury, J., Snyderman, R., & Takai, Y. (1992). Both stimulatory and inhibitory GDP GTP exchange proteins, smg GDS and rho GDI, are active on multiple small GTP-binding proteins. Biochemical and Biophysical Research Communications, 182(2), 921-930. https://doi.org/10.1016/0006-291X(92)91820-G

Hiraoka, Kunihiko ; Kaibuchi, Kozo ; Ando, Satoshi ; Musha, Takashi ; Takaishi, Kenji ; Mizuno, Takakazu ; Asada, Makoto ; Ménard, Luc ; Tomhave, Eric ; Didsbury, John ; Snyderman, Ralph ; Takai, Yoshimi. / Both stimulatory and inhibitory GDP GTP exchange proteins, smg GDS and rho GDI, are active on multiple small GTP-binding proteins. In: Biochemical and Biophysical Research Communications. 1992 ; Vol. 182, No. 2. pp. 921-930.

@article{0f6b3491f85641edbfc582d7f0c2f67f,

title = "Both stimulatory and inhibitory GDP GTP exchange proteins, smg GDS and rho GDI, are active on multiple small GTP-binding proteins",

abstract = "Six peaks of small GTP-binding proteins (G proteins) were separated by column chromatographies from the cytosol fraction of the differentiated HL-60 cells: two peaks of rho p21, one peak of smg rap1 p21, two peaks of rac1 p21, and one peak of an unidentified small G protein with a Mr of about 20,000 (20 KG). smg GDS, previously thought to be a stimulatory GDP GTP exchange protein for smg p21, Ki-ras p21, and rho p21, but not for Ha-ras p21 or smg p25A, was also active on rac1 p21. rho GDI, previously thought to be an inhibitory GDP GTP exchange protein specific for rho p21, was also active on rac1 p21. These results indicate that both smg GDS and rho GDI are active on multiple small G proteins.",

author = "Kunihiko Hiraoka and Kozo Kaibuchi and Satoshi Ando and Takashi Musha and Kenji Takaishi and Takakazu Mizuno and Makoto Asada and Luc M{\'e}nard and Eric Tomhave and John Didsbury and Ralph Snyderman and Yoshimi Takai",

note = "Funding Information: ' The investigation at Kobe University was supported by grants-in-aid for Scientific Research and for Cancer Research the Ministry of Education, Science, and Culture, Japan (1991), grants-in-aid for Abnormalities in Hormone Receptor Mechanisms for Aging and Health from the Ministry of Health and Welfare, (1991) I and grants from the Yamanouchi Foundation for Research Metabolic Disease (1991) and from the Research Program on Cell Calcium Signal in the Cardiovascular System (1991).",

year = "1992",

month = jan,

day = "31",

doi = "10.1016/0006-291X(92)91820-G",

language = "English",

volume = "182",

pages = "921--930",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "2",

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Hiraoka, K, Kaibuchi, K, Ando, S, Musha, T, Takaishi, K, Mizuno, T, Asada, M, Ménard, L, Tomhave, E, Didsbury, J, Snyderman, R & Takai, Y 1992, 'Both stimulatory and inhibitory GDP GTP exchange proteins, smg GDS and rho GDI, are active on multiple small GTP-binding proteins', Biochemical and Biophysical Research Communications, vol. 182, no. 2, pp. 921-930. https://doi.org/10.1016/0006-291X(92)91820-G

Both stimulatory and inhibitory GDP GTP exchange proteins, smg GDS and rho GDI, are active on multiple small GTP-binding proteins. / Hiraoka, Kunihiko; Kaibuchi, Kozo; Ando, Satoshi; Musha, Takashi; Takaishi, Kenji; Mizuno, Takakazu; Asada, Makoto; Ménard, Luc; Tomhave, Eric; Didsbury, John; Snyderman, Ralph; Takai, Yoshimi.

In: Biochemical and Biophysical Research Communications, Vol. 182, No. 2, 31.01.1992, p. 921-930.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Both stimulatory and inhibitory GDP GTP exchange proteins, smg GDS and rho GDI, are active on multiple small GTP-binding proteins

AU - Hiraoka, Kunihiko

AU - Kaibuchi, Kozo

AU - Ando, Satoshi

AU - Musha, Takashi

AU - Takaishi, Kenji

AU - Mizuno, Takakazu

AU - Asada, Makoto

AU - Ménard, Luc

AU - Tomhave, Eric

AU - Didsbury, John

AU - Snyderman, Ralph

AU - Takai, Yoshimi

N1 - Funding Information: ' The investigation at Kobe University was supported by grants-in-aid for Scientific Research and for Cancer Research the Ministry of Education, Science, and Culture, Japan (1991), grants-in-aid for Abnormalities in Hormone Receptor Mechanisms for Aging and Health from the Ministry of Health and Welfare, (1991) I and grants from the Yamanouchi Foundation for Research Metabolic Disease (1991) and from the Research Program on Cell Calcium Signal in the Cardiovascular System (1991).

PY - 1992/1/31

Y1 - 1992/1/31

N2 - Six peaks of small GTP-binding proteins (G proteins) were separated by column chromatographies from the cytosol fraction of the differentiated HL-60 cells: two peaks of rho p21, one peak of smg rap1 p21, two peaks of rac1 p21, and one peak of an unidentified small G protein with a Mr of about 20,000 (20 KG). smg GDS, previously thought to be a stimulatory GDP GTP exchange protein for smg p21, Ki-ras p21, and rho p21, but not for Ha-ras p21 or smg p25A, was also active on rac1 p21. rho GDI, previously thought to be an inhibitory GDP GTP exchange protein specific for rho p21, was also active on rac1 p21. These results indicate that both smg GDS and rho GDI are active on multiple small G proteins.

AB - Six peaks of small GTP-binding proteins (G proteins) were separated by column chromatographies from the cytosol fraction of the differentiated HL-60 cells: two peaks of rho p21, one peak of smg rap1 p21, two peaks of rac1 p21, and one peak of an unidentified small G protein with a Mr of about 20,000 (20 KG). smg GDS, previously thought to be a stimulatory GDP GTP exchange protein for smg p21, Ki-ras p21, and rho p21, but not for Ha-ras p21 or smg p25A, was also active on rac1 p21. rho GDI, previously thought to be an inhibitory GDP GTP exchange protein specific for rho p21, was also active on rac1 p21. These results indicate that both smg GDS and rho GDI are active on multiple small G proteins.

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U2 - 10.1016/0006-291X(92)91820-G

DO - 10.1016/0006-291X(92)91820-G

M3 - Article

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AN - SCOPUS:0026501099

VL - 182

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EP - 930

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -

Both stimulatory and inhibitory GDP GTP exchange proteins, smg GDS and rho GDI, are active on multiple small GTP-binding proteins

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