Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0014-5793(03)00213-8
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dc.titleArhGAP15, a novel human RacGAP protein with GTPase binding property
dc.contributor.authorSeoh, M.L.
dc.contributor.authorNg, C.H.
dc.contributor.authorYong, J.
dc.contributor.authorLim, L.
dc.contributor.authorLeung, T.
dc.date.accessioned2014-12-01T06:57:39Z
dc.date.available2014-12-01T06:57:39Z
dc.date.issued2003-03-27
dc.identifier.citationSeoh, 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
dc.identifier.issn00145793
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/113718
dc.description.abstractWe 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0014-5793(03)00213-8
dc.sourceScopus
dc.subjectActin cytoskeleton
dc.subjectGAP
dc.subjectRac1
dc.subjectRac1-binding
dc.typeConference Paper
dc.contributor.departmentANATOMY
dc.description.doi10.1016/S0014-5793(03)00213-8
dc.description.sourcetitleFEBS Letters
dc.description.volume539
dc.description.issue1-3
dc.description.page131-137
dc.description.codenFEBLA
dc.identifier.isiut000181957400026
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