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Actin Engine in Immunological Synapse

T cell activation and function require physical contact with antigen presenting cells at a specialized junctional structure known as the immunological synapse. Once formed, the immunological synapse leads to sustained T cell receptor-mediated signalling and stabilized adhesion. High resolution micro...

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Detalles Bibliográficos
Autores principales: Piragyte, Indre, Jun, Chang-Duk
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Korean Association of Immunologists 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3422712/
https://www.ncbi.nlm.nih.gov/pubmed/22916042
http://dx.doi.org/10.4110/in.2012.12.3.71
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author Piragyte, Indre
Jun, Chang-Duk
author_facet Piragyte, Indre
Jun, Chang-Duk
author_sort Piragyte, Indre
collection PubMed
description T cell activation and function require physical contact with antigen presenting cells at a specialized junctional structure known as the immunological synapse. Once formed, the immunological synapse leads to sustained T cell receptor-mediated signalling and stabilized adhesion. High resolution microscopy indeed had a great impact in understanding the function and dynamic structure of immunological synapse. Trends of recent research are now moving towards understanding the mechanical part of immune system, expanding our knowledge in mechanosensitivity, force generation, and biophysics of cell-cell interaction. Actin cytoskeleton plays inevitable role in adaptive immune system, allowing it to bear dynamic and precise characteristics at the same time. The regulation of mechanical engine seems very complicated and overlapping, but it enables cells to be very sensitive to external signals such as surface rigidity. In this review, we focus on actin regulators and how immune cells regulate dynamic actin rearrangement process to drive the formation of immunological synapse.
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spelling pubmed-34227122012-08-22 Actin Engine in Immunological Synapse Piragyte, Indre Jun, Chang-Duk Immune Netw Review Article T cell activation and function require physical contact with antigen presenting cells at a specialized junctional structure known as the immunological synapse. Once formed, the immunological synapse leads to sustained T cell receptor-mediated signalling and stabilized adhesion. High resolution microscopy indeed had a great impact in understanding the function and dynamic structure of immunological synapse. Trends of recent research are now moving towards understanding the mechanical part of immune system, expanding our knowledge in mechanosensitivity, force generation, and biophysics of cell-cell interaction. Actin cytoskeleton plays inevitable role in adaptive immune system, allowing it to bear dynamic and precise characteristics at the same time. The regulation of mechanical engine seems very complicated and overlapping, but it enables cells to be very sensitive to external signals such as surface rigidity. In this review, we focus on actin regulators and how immune cells regulate dynamic actin rearrangement process to drive the formation of immunological synapse. The Korean Association of Immunologists 2012-06 2012-06-30 /pmc/articles/PMC3422712/ /pubmed/22916042 http://dx.doi.org/10.4110/in.2012.12.3.71 Text en Copyright © 2012 The Korean Association of Immunologists http://creativecommons.org/licenses/by-nc/3.0 This is an open access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Piragyte, Indre
Jun, Chang-Duk
Actin Engine in Immunological Synapse
title Actin Engine in Immunological Synapse
title_full Actin Engine in Immunological Synapse
title_fullStr Actin Engine in Immunological Synapse
title_full_unstemmed Actin Engine in Immunological Synapse
title_short Actin Engine in Immunological Synapse
title_sort actin engine in immunological synapse
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3422712/
https://www.ncbi.nlm.nih.gov/pubmed/22916042
http://dx.doi.org/10.4110/in.2012.12.3.71
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