β3-Chimaerin, a novel member of the chimaerin Rac-GAP family

Chimaerins are a family of diacylglycerol- and phorbol ester-regulated GTPase activating proteins (GAPs) for the small G-protein Rac. Extensive evidence indicates that these proteins play important roles in development, axon guidance, metabolism, cell motility, and T cell activation. Four isoforms h...

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Autor principal: Zubeldia-Brenner, L.
Otros Autores: Gutierrez-Uzquiza, A., Barrio-Real, L., Wang, H., Kazanietz, M.G, Leskow, F.C
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2014
Acceso en línea:Registro en Scopus
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Aporte de:Registro referencial: Solicitar el recurso aquí
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100 1 |a Zubeldia-Brenner, L. 
245 1 0 |a β3-Chimaerin, a novel member of the chimaerin Rac-GAP family 
260 |c 2014 
270 1 0 |m Leskow, F.C.; Departamento de Ciencias Básicas, Universidad Nacional de Luján, Luján, 6700, Buenos Aires, Argentina; email: federico@fbmc.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
520 3 |a Chimaerins are a family of diacylglycerol- and phorbol ester-regulated GTPase activating proteins (GAPs) for the small G-protein Rac. Extensive evidence indicates that these proteins play important roles in development, axon guidance, metabolism, cell motility, and T cell activation. Four isoforms have been reported to-date, which are products of CHN1 (α1- and α2-chimaerins) and CHN2 (β1- and β2-chimaerins) genes. Although these gene products are assumed to be generated by alternative splicing, bioinformatics analysis of the CHN2 gene revealed that β1- and β2-chimaerins are the products of alternative transcription start sites (TSSs) in different promoter regions. Furthermore, we found an additional TSS in CHN2 gene that leads to a novel product, which we named β3-chimaerin. Expression profile analysis revealed predominantly low levels for the β3-chimaerin transcript, with higher expression levels in epididymis, plasma blood leucocytes, spleen, thymus, as well as various areas of the brain. In addition to the prototypical SH2, C1, and Rac-GAP domains, β3-chimaerin has a unique N-terminal domain. Studies in cells established that β3-chimaerin has Rac-GAP activity and is responsive to phorbol esters. The enhanced responsiveness of β3-chimaerin for phorbol ester-induced translocation relative to β2-chimaerin suggests differential ligand accessibility to the C1 domain. © 2014 Springer Science+Business Media Dordrecht.  |l eng 
536 |a Article in Press 
593 |a Departamento de Quimica Biologica, Facultad de Ciencias Exactas y Naturales, IQUIBICEN-CONICET, Universidad de Buenos Aires, Buenos Aires, C1428EGA, Argentina 
593 |a Department of Pharmacology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, 19104-6160, United States 
593 |a Departamento de Ciencias Básicas, Universidad Nacional de Luján, Luján, 6700, Argentina 
690 1 0 |a C1 DOMAIN 
690 1 0 |a CHIMAERIN 
690 1 0 |a CHN2 
690 1 0 |a PHORBOL ESTERS 
690 1 0 |a RAC-GAP 
700 1 |a Gutierrez-Uzquiza, A. 
700 1 |a Barrio-Real, L. 
700 1 |a Wang, H. 
700 1 |a Kazanietz, M.G. 
700 1 |a Leskow, F.C. 
773 0 |d 2014  |h pp. 1-10  |p Mol. Biol. Rep.  |x 03014851  |w (AR-BaUEN)CENRE-3497  |t Molecular Biology Reports 
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