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Focal Adhesion Kinases in Adhesion Structures and Disease
Cell adhesion to the extracellular matrix (ECM) is essential for cell migration, proliferation, and embryonic development. Cells can contact the ECM through a wide range of matrix contact structures such as focal adhesions, podosomes, and invadopodia. Although they are different in structural design...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3409539/ https://www.ncbi.nlm.nih.gov/pubmed/22888421 http://dx.doi.org/10.1155/2012/296450 |
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author | Eleniste, Pierre P. Bruzzaniti, Angela |
author_facet | Eleniste, Pierre P. Bruzzaniti, Angela |
author_sort | Eleniste, Pierre P. |
collection | PubMed |
description | Cell adhesion to the extracellular matrix (ECM) is essential for cell migration, proliferation, and embryonic development. Cells can contact the ECM through a wide range of matrix contact structures such as focal adhesions, podosomes, and invadopodia. Although they are different in structural design and basic function, they share common remodeling proteins such as integrins, talin, paxillin, and the tyrosine kinases FAK, Pyk2, and Src. In this paper, we compare and contrast the basic organization and role of focal adhesions, podosomes, and invadopodia in different cells. In addition, we discuss the role of the tyrosine kinases, FAK, Pyk2, and Src, which are critical for the function of the different adhesion structures. Finally, we discuss the essential role of these tyrosine kinases from the perspective of human diseases. |
format | Online Article Text |
id | pubmed-3409539 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-34095392012-08-10 Focal Adhesion Kinases in Adhesion Structures and Disease Eleniste, Pierre P. Bruzzaniti, Angela J Signal Transduct Review Article Cell adhesion to the extracellular matrix (ECM) is essential for cell migration, proliferation, and embryonic development. Cells can contact the ECM through a wide range of matrix contact structures such as focal adhesions, podosomes, and invadopodia. Although they are different in structural design and basic function, they share common remodeling proteins such as integrins, talin, paxillin, and the tyrosine kinases FAK, Pyk2, and Src. In this paper, we compare and contrast the basic organization and role of focal adhesions, podosomes, and invadopodia in different cells. In addition, we discuss the role of the tyrosine kinases, FAK, Pyk2, and Src, which are critical for the function of the different adhesion structures. Finally, we discuss the essential role of these tyrosine kinases from the perspective of human diseases. Hindawi Publishing Corporation 2012 2012-07-19 /pmc/articles/PMC3409539/ /pubmed/22888421 http://dx.doi.org/10.1155/2012/296450 Text en Copyright © 2012 P. P. Eleniste and A. Bruzzaniti. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Eleniste, Pierre P. Bruzzaniti, Angela Focal Adhesion Kinases in Adhesion Structures and Disease |
title | Focal Adhesion Kinases in Adhesion Structures and Disease |
title_full | Focal Adhesion Kinases in Adhesion Structures and Disease |
title_fullStr | Focal Adhesion Kinases in Adhesion Structures and Disease |
title_full_unstemmed | Focal Adhesion Kinases in Adhesion Structures and Disease |
title_short | Focal Adhesion Kinases in Adhesion Structures and Disease |
title_sort | focal adhesion kinases in adhesion structures and disease |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3409539/ https://www.ncbi.nlm.nih.gov/pubmed/22888421 http://dx.doi.org/10.1155/2012/296450 |
work_keys_str_mv | AT elenistepierrep focaladhesionkinasesinadhesionstructuresanddisease AT bruzzanitiangela focaladhesionkinasesinadhesionstructuresanddisease |