Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0014-5793(03)00213-8
Title: ArhGAP15, a novel human RacGAP protein with GTPase binding property
Authors: Seoh, M.L.
Ng, C.H.
Yong, J.
Lim, L.
Leung, T. 
Keywords: Actin cytoskeleton
GAP
Rac1
Rac1-binding
Issue Date: 27-Mar-2003
Citation: Seoh, M.L., Ng, C.H., Yong, J., Lim, L., Leung, T. (2003-03-27). ArhGAP15, a novel human RacGAP protein with GTPase binding property. FEBS Letters 539 (1-3) : 131-137. ScholarBank@NUS Repository. https://doi.org/10.1016/S0014-5793(03)00213-8
Abstract: We have previously described a partial cDNA sequence encoding a RhoGAP protein, GAP25 that is homologous to the recently reported ArhGAP9 and ArhGAP12. We now describe a related new member ArhGAP15 that shares a number of domain similarities, including a pleckstrin homology (PH) domain, a RhoGAP domain and a novel motif N-terminal to the GAP domain. This novel motif was found to be responsible for nucleotide-independent Rac1 binding. Using swop mutants of Rac/Cdc42, we have established that the binding is through the C-terminal half of Rac1. The GAP domain of ArhGAP15 showed specificity towards Rac1 in vitro. The PH domain is required for ArhGAP15 to localize to cell periphery and over-expression of the full-length ArhGAP15, but not the mutant with a partial deletion of the PH domain, resulted in an increase in actin stress fibers and cell contraction. These morphological effects can be attenuated by the co-expression of dominant negative Rac1N17. HeLa cells expressing ArhGAP15 were also resistant to phorbol myristatate acetate treatment, suggesting that ArhGAP15 is a potential regulator of Rac1. © 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
Source Title: FEBS Letters
URI: http://scholarbank.nus.edu.sg/handle/10635/113718
ISSN: 00145793
DOI: 10.1016/S0014-5793(03)00213-8
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