Trends in Genetics
ReviewGAPs for rho-related GTPases
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Cited by (214)
Rac-dependent feedforward autoactivation of NOX2 leads to oxidative burst
2021, Journal of Biological ChemistryDeciphering the molecular and functional basis of RHOGAP family proteins: A systematic approach toward selective inactivation of RHO family proteins
2016, Journal of Biological ChemistryCitation Excerpt :Most remarkably, the same mechanistic strategy has been shown for bacterial GAPs, such as the Salmonella typhimurium virulence factor SptP, the Pseudomonas aeruginosa cytotoxin ExoS, and the Yersinia pestis YopE, even though they do not share any sequence or structural similarities with eukaryotic RHOGAP domains (15–17). Mining in the UniProt database led to the identification of 66 distinct human proteins containing a common RHOGAP domain (Fig. 1; Table 1), a number that is slightly different from previous reports (18–25). Among them p50RHOGAP (26), also known as CDC42GAP (27), p190 (28), and BCR (29) were the first identified and also the best characterized family members.
Thiopurine prodrugs mediate immunosuppressive effects by interfering with Rac1 protein function
2016, Journal of Biological ChemistryCitation Excerpt :Both GDP- and GTP-bound Rac1 exist in cells. By assuming that the metabolic process of 6-TG is similar to the guanine base, it is possible to speculate that the biologically active 6-TGTP-Rac1 adduct, in addition to the biologically inactive 6-TGDP-Rac1 adduct, may also exist in CD4+ cells treated with 6-TG and/or DETA/NO. If so, the mechanism of the conversion of the 6-TGTP-Rac1 adduct into the 6-TGDP-Rac1 adduct is of interest because only the 6-TGDP-Rac1 adduct is populated in CD4+ cells treated with 6-TG and/or DETA/NO. It has been shown that the catalytic action of RhoGAP on GTPase is the main factor that converts the active GTP-bound form of Rac1 into the inactive GDP-bound Rac1 (39, 40). Hence, the catalytic activity of RhoGAP on the 6-TGTP-Rac1 adduct was examined to recognize the mechanism for the dominant population of the 6-TGDP-Rac1 adduct in CD4+ cells treated with 6-TG and/or DETA/NO. As with the above fluorescence analysis, the 6-TGDP- and 6-TGTP-Rac1 adducts were prepared from Rac1 that was expressed in and purified from E. coli.
Cell type-Specific signaling function of rhoa gtpase: Lessons from mouse genetargeting
2013, Journal of Biological ChemistryArhGAP15, a rac-specific gtpase-activating protein, plays a dual role in inhibiting small GTpase signaling
2013, Journal of Biological Chemistry