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Research advances on structure and biological functions of integrins
Integrins are an important family of adhesion molecules that were first discovered two decades ago. Integrins are transmembrane heterodimeric glycoprotein receptors consisting of α and β subunits, and are comprised of an extracellular domain, a transmembrane domain, and a cytoplasmic tail. Therein,...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4947080/ https://www.ncbi.nlm.nih.gov/pubmed/27468395 http://dx.doi.org/10.1186/s40064-016-2502-0 |
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author | Pan, Li Zhao, Yuan Yuan, Zhijie Qin, Guixin |
author_facet | Pan, Li Zhao, Yuan Yuan, Zhijie Qin, Guixin |
author_sort | Pan, Li |
collection | PubMed |
description | Integrins are an important family of adhesion molecules that were first discovered two decades ago. Integrins are transmembrane heterodimeric glycoprotein receptors consisting of α and β subunits, and are comprised of an extracellular domain, a transmembrane domain, and a cytoplasmic tail. Therein, integrin cytoplasmic domains may associate directly with numerous cytoskeletal proteins and intracellular signaling molecules, which are crucial for modulating fundamental cell processes and functions including cell adhesion, proliferation, migration, and survival. The purpose of this review is to describe the unique structure of each integrin subunit, primary cytoplasmic association proteins, and transduction signaling pathway of integrins, with an emphasis on their biological functions. |
format | Online Article Text |
id | pubmed-4947080 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-49470802016-07-27 Research advances on structure and biological functions of integrins Pan, Li Zhao, Yuan Yuan, Zhijie Qin, Guixin Springerplus Review Integrins are an important family of adhesion molecules that were first discovered two decades ago. Integrins are transmembrane heterodimeric glycoprotein receptors consisting of α and β subunits, and are comprised of an extracellular domain, a transmembrane domain, and a cytoplasmic tail. Therein, integrin cytoplasmic domains may associate directly with numerous cytoskeletal proteins and intracellular signaling molecules, which are crucial for modulating fundamental cell processes and functions including cell adhesion, proliferation, migration, and survival. The purpose of this review is to describe the unique structure of each integrin subunit, primary cytoplasmic association proteins, and transduction signaling pathway of integrins, with an emphasis on their biological functions. Springer International Publishing 2016-07-15 /pmc/articles/PMC4947080/ /pubmed/27468395 http://dx.doi.org/10.1186/s40064-016-2502-0 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Review Pan, Li Zhao, Yuan Yuan, Zhijie Qin, Guixin Research advances on structure and biological functions of integrins |
title | Research advances on structure and biological functions of integrins |
title_full | Research advances on structure and biological functions of integrins |
title_fullStr | Research advances on structure and biological functions of integrins |
title_full_unstemmed | Research advances on structure and biological functions of integrins |
title_short | Research advances on structure and biological functions of integrins |
title_sort | research advances on structure and biological functions of integrins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4947080/ https://www.ncbi.nlm.nih.gov/pubmed/27468395 http://dx.doi.org/10.1186/s40064-016-2502-0 |
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