Characterization of a GTPase-activating protein for the Ras-related Ral protein
نویسندگان
چکیده
منابع مشابه
Purification of ras GTPase activating protein from bovine brain.
In cytosolic extracts of bovine brain, we detected ras GTPase activating protein (GAP) activity that stimulated the GTP hydrolytic activity of normal c-Ha-ras p21 but not that of the oncogenic [Val12]p21 variant. GAP was purified 19,500-fold by a five-column procedure involving DEAE-Sephacel, Sepharose 6B, orange dye and green dye matrices, and Mono Q resins. A single major protein band of 125 ...
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Rho small GTPases control multiple aspects of neuronal morphogenesis by regulating the assembly and organization of the actin cytoskeleton. Although they are negatively regulated by GTPase activating proteins (GAPs), the roles of RhoGAPs in the nervous system have not been fully investigated. Here we describe a characterization of Drosophila RhoGAP68F that is mainly expressed in the embryonic c...
متن کاملPurification and functional reconstitution of intact ral-binding Gtpase activating protein, RLIP76, in artificial liposomes.
We have recently shown that RLIP76, a ral-binding GTPase activating protein, mediates ATP-dependent transport of glutathione-conjugates (GS-E) and doxorubicin (DOX) (S. Awasthi et al., Biochemistry 39,9327,2000). Transport function of RLIP76 was found to be intact despite considerable proteolytic fragmentation in preparations used for those studies, suggesting either that the residual intact RL...
متن کاملEpidermal growth factor increases protein and messenger RNA expression levels of Ras GTPase activating protein.
The Ras GTPase activating protein (RasGAP) is a key regulatory enzyme in the Ras signaling pathway, which is crucial for growth factor-induced mitogenesis. In this study, it is shown that epidermal growth factor (EGF) increases RasGAP protein expression by 100-150% in NIH 3T3 cells, which overexpress the human EGF receptor, and mouse keratinocytes but does not increase RasGAP protein expression...
متن کاملTransport functions and physiological significance of 76 kDa Ral-binding GTPase activating protein (RLIP76).
We have recently demonstrated that a previously known Ral-binding GTPase activating protein, RLIP76, can also catalyze ATP-dependent transport of various structurally unrelated xeno- and endobiotics irrespective of their net charge (Awasthi et al., 2000, Biochemistry, 39: 9327). RLIP76 is a non-ATP binding cassette (ABC) protein but it has two ATP-binding sites and shows basal ATPase activity w...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)92877-2