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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| Formato: | INPR |
| Lenguaje: | English |
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_03014851_v_n_p1_ZubeldiaBrenner |
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todo:paper_03014851_v_n_p1_ZubeldiaBrenner2023-10-03T15:18:29Z β3-Chimaerin, a novel member of the chimaerin Rac-GAP family Zubeldia-Brenner, L. Gutierrez-Uzquiza, A. Barrio-Real, L. Wang, H. Kazanietz, M.G. Leskow, F.C. 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. INPR English info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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) |
| language |
English |
| orig_language_str_mv |
English |
| topic |
C1 domain Chimaerin CHN2 Phorbol esters Rac-GAP |
| spellingShingle |
C1 domain Chimaerin CHN2 Phorbol esters Rac-GAP Zubeldia-Brenner, L. Gutierrez-Uzquiza, A. Barrio-Real, L. Wang, H. Kazanietz, M.G. Leskow, F.C. 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. |
| format |
INPR |
| author |
Zubeldia-Brenner, L. Gutierrez-Uzquiza, A. Barrio-Real, L. Wang, H. Kazanietz, M.G. Leskow, F.C. |
| author_facet |
Zubeldia-Brenner, L. Gutierrez-Uzquiza, A. Barrio-Real, L. Wang, H. Kazanietz, M.G. Leskow, F.C. |
| author_sort |
Zubeldia-Brenner, L. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_03014851_v_n_p1_ZubeldiaBrenner |
| work_keys_str_mv |
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