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Title

ß2-chimaerin subcellular localization modulates Rac-mediated responses

AuthorsCasado, Victoria ; Caloca, María J.
Issue Date2012
Citation22nd IUBMB - 37th FEBS Congress (2012)
AbstractChimaerins are a family of GTPase-activating proteins that inactivate the Rac GTPase in a diacylglycerol (DAG) dependent manner. This family is composed of four members, α1-and α2-chimaerin that originate from the CHN1 gene and ß1- and ß2-chimaerin which are products of the CHN2 gene. All chimaerin isoforms have a C1 domain, highly homologous to that of PKC isozymes and a catalytic GAP domain. α2- and ß2-chimaerins have also an N-terminal SH2 domain, most likely involved in heteromolecular interactions. According to the established model for chimaerin activation, it has been shown that EGF redistributes ß2-chimaerin to promote its association with Rac at the plasma membrane. In addition, ß2-chimaerin shows a perinuclear and Golgi localization in response to PMA treatment or after stimulation with EGF. These data suggest that the localization of chimaerins in different subcellular compartments may serve as a mechanism that regulates Rac responses in localized regions of the cell. To study the functional effect of the different cellular localizations of chimaerins we have analyzed the activity of ß2- chimaerin that we have artificially targeted to cell membrane, Golgi and endoplasmic reticulum. Our preliminary results indicate that ß2-chimaerin localized at the plasma membrane participate in the control of actin cytoskeleton and alters cell adherence. This effect is specific of ß2-chimaerin localized at the lipid raft, while targeting ß2-chimaerin to the disordered membrane does not impact on actin cytoskeleton organization. These preliminary data suggest that chimaerins subcellular localization determines the biological outcome of Rac site-specific signals.
DescriptionResumen del póster presentado al 22nd IUBMB & 37th FEBS Congress: "From Single Molecules to Systems Biology" celebrado en Sevilla (España) del 4 al 9 de septiembre de 2012.
URIhttp://hdl.handle.net/10261/117225
Appears in Collections:(IBGM) Comunicaciones congresos
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