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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Detalles Bibliográficos
Publicado: 2014
Materias:
C1 domain
Chimaerin
CHN2
Phorbol esters
Rac-GAP
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03014851_v_n_p1_ZubeldiaBrenner
http://hdl.handle.net/20.500.12110/paper_03014851_v_n_p1_ZubeldiaBrenner
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_03014851_v_n_p1_ZubeldiaBrenner
record_format dspace
spelling paper:paper_03014851_v_n_p1_ZubeldiaBrenner2023-06-08T15:28:01Z β3-Chimaerin, a novel member of the chimaerin Rac-GAP family C1 domain Chimaerin CHN2 Phorbol esters Rac-GAP 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. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03014851_v_n_p1_ZubeldiaBrenner http://hdl.handle.net/20.500.12110/paper_03014851_v_n_p1_ZubeldiaBrenner
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic C1 domain
Chimaerin
CHN2
Phorbol esters
Rac-GAP
spellingShingle C1 domain
Chimaerin
CHN2
Phorbol esters
Rac-GAP
β3-Chimaerin, a novel member of the chimaerin Rac-GAP family
topic_facet C1 domain
Chimaerin
CHN2
Phorbol esters
Rac-GAP
description 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.
title β3-Chimaerin, a novel member of the chimaerin Rac-GAP family
title_short β3-Chimaerin, a novel member of the chimaerin Rac-GAP family
title_full β3-Chimaerin, a novel member of the chimaerin Rac-GAP family
title_fullStr β3-Chimaerin, a novel member of the chimaerin Rac-GAP family
title_full_unstemmed β3-Chimaerin, a novel member of the chimaerin Rac-GAP family
title_sort β3-chimaerin, a novel member of the chimaerin rac-gap family
publishDate 2014
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03014851_v_n_p1_ZubeldiaBrenner
http://hdl.handle.net/20.500.12110/paper_03014851_v_n_p1_ZubeldiaBrenner
_version_ 1768546252006359040

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