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Cited by 75

The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.

Regulation of RhoA GTP Hydrolysis by the GTPase-Activating Proteins p190, p50RhoGAP, Bcr, and 3BP-1

Zhang, Baolin, Zheng, Yi·1998·Biochemistry
DOI 10.1021/bi9718447
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Abstract

The small GTP-binding protein RhoA becomes inactivated by hydrolyzing bound GTP to GDP through its intrinsic GTPase activity which is further stimulated by a family of Rho GTPase-activating proteins (GAPs). Here we have compared the kinetics of interaction between recombinant RhoA and the RhoGAP domains of p190, p50RhoGAP, Bcr, and 3BP-1. The intrinsic rate of GTP hydrolysis by RhoA is relatively slow when compared to other Rho-family GTPases such as Cdc42 or Rac1 with a rate constant of 0.022 min-1, which can be further stimulated at least 4000-fold by p190 or p50RhoGAP. The RhoGAP domains of Bcr and 3BP-1, which were thought to be inactive toward RhoA, are also found capable of stimulating the GTPase activity of RhoA in a dose-dependent manner. The supreme catalytic activities of p190 and p50RhoGAP toward RhoA reside mostly in their lower Km values (1.79 and 2.83 microM, respectively) which correlate well with their binding affinity for GMP-PNP-bound RhoA (2.18 and 2. 47 microM, respectively), in contrast with Bcr and 3BP-1 which interact with the activated RhoA with much higher Km (89 microM). However, the mechanisms of catalysis by p190 and p50RhoGAP are distinct in at least three aspects: (1) p50RhoGAP displays an effect of product inhibition by binding to the GDP-bound form of RhoA with a Kd of 6 microM in comparison with the Kd for p190 of 33 microM; (2) the Km of p190 increases drastically upon the increase of salt and Mg2+ concentrations, conditions under which only…

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Citations

Cites

Research works printed but not linked: 34

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Metadata

Authors
Zhang, B., & Zheng, Y.
Affiliations
Department of Biochemistry, University of Tennessee, Memphis, Tennessee 38163
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1998-03-24
Volume
37
Issue
15
Pages
5249-5257
ISSN
  • 0006-2960
  • 1520-4995
DOI
10.1021/bi9718447
Cited by
75
References
14
Language
en

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