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Centrosome Polarization in T Cells: A Task for Formins

T-cell antigen receptor (TCR) engagement triggers the rapid reorientation of the centrosome, which is associated with the secretory machinery, toward the immunological synapse (IS) for polarized protein trafficking. Recent evidence indicates that upon TCR triggering the INF2 formin, together with th...

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Autores principales: Andrés-Delgado, Laura, Antón, Olga M., Alonso, Miguel Angel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3708132/
https://www.ncbi.nlm.nih.gov/pubmed/23874337
http://dx.doi.org/10.3389/fimmu.2013.00191
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author Andrés-Delgado, Laura
Antón, Olga M.
Alonso, Miguel Angel
author_facet Andrés-Delgado, Laura
Antón, Olga M.
Alonso, Miguel Angel
author_sort Andrés-Delgado, Laura
collection PubMed
description T-cell antigen receptor (TCR) engagement triggers the rapid reorientation of the centrosome, which is associated with the secretory machinery, toward the immunological synapse (IS) for polarized protein trafficking. Recent evidence indicates that upon TCR triggering the INF2 formin, together with the formins DIA1 and FMNL1, promotes the formation of a specialized array of stable detyrosinated MTs that breaks the symmetrical organization of the T-cell microtubule (MT) cytoskeleton. The detyrosinated MT array and TCR-induced tyrosine phosphorylation should coincide for centrosome polarization. We propose that the pushing forces produced by the detyrosinated MT array, which modify the position of the centrosome, in concert with Src kinase dependent TCR signaling, which provide the reference frame with respect to which the centrosome reorients, result in the repositioning of the centrosome to the IS.
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spelling pubmed-37081322013-07-19 Centrosome Polarization in T Cells: A Task for Formins Andrés-Delgado, Laura Antón, Olga M. Alonso, Miguel Angel Front Immunol Immunology T-cell antigen receptor (TCR) engagement triggers the rapid reorientation of the centrosome, which is associated with the secretory machinery, toward the immunological synapse (IS) for polarized protein trafficking. Recent evidence indicates that upon TCR triggering the INF2 formin, together with the formins DIA1 and FMNL1, promotes the formation of a specialized array of stable detyrosinated MTs that breaks the symmetrical organization of the T-cell microtubule (MT) cytoskeleton. The detyrosinated MT array and TCR-induced tyrosine phosphorylation should coincide for centrosome polarization. We propose that the pushing forces produced by the detyrosinated MT array, which modify the position of the centrosome, in concert with Src kinase dependent TCR signaling, which provide the reference frame with respect to which the centrosome reorients, result in the repositioning of the centrosome to the IS. Frontiers Media S.A. 2013-07-11 /pmc/articles/PMC3708132/ /pubmed/23874337 http://dx.doi.org/10.3389/fimmu.2013.00191 Text en Copyright © 2013 Andrés-Delgado, Antón and Alonso. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc.
spellingShingle Immunology
Andrés-Delgado, Laura
Antón, Olga M.
Alonso, Miguel Angel
Centrosome Polarization in T Cells: A Task for Formins
title Centrosome Polarization in T Cells: A Task for Formins
title_full Centrosome Polarization in T Cells: A Task for Formins
title_fullStr Centrosome Polarization in T Cells: A Task for Formins
title_full_unstemmed Centrosome Polarization in T Cells: A Task for Formins
title_short Centrosome Polarization in T Cells: A Task for Formins
title_sort centrosome polarization in t cells: a task for formins
topic Immunology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3708132/
https://www.ncbi.nlm.nih.gov/pubmed/23874337
http://dx.doi.org/10.3389/fimmu.2013.00191
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