Consequences of weak interaction of rho GDI with the GTP-bound forms of rho p21 and rac p21

T. Sasaki, Masaki Kato, Y. Takai

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

rho GDI is an inhibitory GDP/GTP exchange protein for the rho family. Recently, rho GDI has been reported to interact with the GTP-bound form of G25K and rac1 p21 and to inhibit their basal and GTPase-activating protein (GAP)-stimulated GTPase activity. Here, we examined whether rho GDI interacts with the GTP-bound form of rho p21 and rac p21 and inhibits their basal and rho GAP-stimulated GTPase activity. rho GDI interacted with both the GDP- and GTP-bound forms of rhoA p21 and rac1 p21 as estimated by measuring its ability to form a complex with both forms and to inhibit the membrane- binding activity of both forms. The efficiency of rho GDI for interaction with the GTP-bound form was, however, about 10% that for interaction with the GDP-bound form. Moreover, rho GDI inhibited both the basal and rho GAP- stimulated GTPase activity of rhoA p21 and rac1 p21 in a dose-dependent manner. The doses of rho GDI necessary for this action were, however, about 10-fold higher than those necessary for the action to inhibit their GDP/GTP exchange reaction. These results indicate that rho GDI interacts with the GTP-bound form of its substrate small G proteins, as well as with the GDP- bound form, but much less efficiently than with the GDP-bound form.

Original languageEnglish
Pages (from-to)23959-23963
Number of pages5
JournalJournal of Biological Chemistry
Volume268
Issue number32
Publication statusPublished - 1993
Externally publishedYes

Fingerprint

rho-Specific Guanine Nucleotide Dissociation Inhibitors
Guanosine Triphosphate
GTP Phosphohydrolases
GTPase-Activating Proteins
Guanine Nucleotide Exchange Factors
Monomeric GTP-Binding Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Consequences of weak interaction of rho GDI with the GTP-bound forms of rho p21 and rac p21. / Sasaki, T.; Kato, Masaki; Takai, Y.

In: Journal of Biological Chemistry, Vol. 268, No. 32, 1993, p. 23959-23963.

Research output: Contribution to journalArticle

@article{fb6ccbbd454a4cb6b907eb0957d64d09,
title = "Consequences of weak interaction of rho GDI with the GTP-bound forms of rho p21 and rac p21",
abstract = "rho GDI is an inhibitory GDP/GTP exchange protein for the rho family. Recently, rho GDI has been reported to interact with the GTP-bound form of G25K and rac1 p21 and to inhibit their basal and GTPase-activating protein (GAP)-stimulated GTPase activity. Here, we examined whether rho GDI interacts with the GTP-bound form of rho p21 and rac p21 and inhibits their basal and rho GAP-stimulated GTPase activity. rho GDI interacted with both the GDP- and GTP-bound forms of rhoA p21 and rac1 p21 as estimated by measuring its ability to form a complex with both forms and to inhibit the membrane- binding activity of both forms. The efficiency of rho GDI for interaction with the GTP-bound form was, however, about 10{\%} that for interaction with the GDP-bound form. Moreover, rho GDI inhibited both the basal and rho GAP- stimulated GTPase activity of rhoA p21 and rac1 p21 in a dose-dependent manner. The doses of rho GDI necessary for this action were, however, about 10-fold higher than those necessary for the action to inhibit their GDP/GTP exchange reaction. These results indicate that rho GDI interacts with the GTP-bound form of its substrate small G proteins, as well as with the GDP- bound form, but much less efficiently than with the GDP-bound form.",
author = "T. Sasaki and Masaki Kato and Y. Takai",
year = "1993",
language = "English",
volume = "268",
pages = "23959--23963",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "32",

}

TY - JOUR

T1 - Consequences of weak interaction of rho GDI with the GTP-bound forms of rho p21 and rac p21

AU - Sasaki, T.

AU - Kato, Masaki

AU - Takai, Y.

PY - 1993

Y1 - 1993

N2 - rho GDI is an inhibitory GDP/GTP exchange protein for the rho family. Recently, rho GDI has been reported to interact with the GTP-bound form of G25K and rac1 p21 and to inhibit their basal and GTPase-activating protein (GAP)-stimulated GTPase activity. Here, we examined whether rho GDI interacts with the GTP-bound form of rho p21 and rac p21 and inhibits their basal and rho GAP-stimulated GTPase activity. rho GDI interacted with both the GDP- and GTP-bound forms of rhoA p21 and rac1 p21 as estimated by measuring its ability to form a complex with both forms and to inhibit the membrane- binding activity of both forms. The efficiency of rho GDI for interaction with the GTP-bound form was, however, about 10% that for interaction with the GDP-bound form. Moreover, rho GDI inhibited both the basal and rho GAP- stimulated GTPase activity of rhoA p21 and rac1 p21 in a dose-dependent manner. The doses of rho GDI necessary for this action were, however, about 10-fold higher than those necessary for the action to inhibit their GDP/GTP exchange reaction. These results indicate that rho GDI interacts with the GTP-bound form of its substrate small G proteins, as well as with the GDP- bound form, but much less efficiently than with the GDP-bound form.

AB - rho GDI is an inhibitory GDP/GTP exchange protein for the rho family. Recently, rho GDI has been reported to interact with the GTP-bound form of G25K and rac1 p21 and to inhibit their basal and GTPase-activating protein (GAP)-stimulated GTPase activity. Here, we examined whether rho GDI interacts with the GTP-bound form of rho p21 and rac p21 and inhibits their basal and rho GAP-stimulated GTPase activity. rho GDI interacted with both the GDP- and GTP-bound forms of rhoA p21 and rac1 p21 as estimated by measuring its ability to form a complex with both forms and to inhibit the membrane- binding activity of both forms. The efficiency of rho GDI for interaction with the GTP-bound form was, however, about 10% that for interaction with the GDP-bound form. Moreover, rho GDI inhibited both the basal and rho GAP- stimulated GTPase activity of rhoA p21 and rac1 p21 in a dose-dependent manner. The doses of rho GDI necessary for this action were, however, about 10-fold higher than those necessary for the action to inhibit their GDP/GTP exchange reaction. These results indicate that rho GDI interacts with the GTP-bound form of its substrate small G proteins, as well as with the GDP- bound form, but much less efficiently than with the GDP-bound form.

UR - http://www.scopus.com/inward/record.url?scp=0027437622&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027437622&partnerID=8YFLogxK

M3 - Article

C2 - 8226937

AN - SCOPUS:0027437622

VL - 268

SP - 23959

EP - 23963

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 32

ER -