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Evolution of complexity in the integrin adhesome
Integrin-mediated adhesion is as ancient as multicellularity, but it was not always as complex as it is in humans. Here, I examine the extent of conservation of 192 adhesome proteins across the genomes of nine model organisms spanning one and a half billion years of evolution. The work reveals that...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2728394/ https://www.ncbi.nlm.nih.gov/pubmed/19667126 http://dx.doi.org/10.1083/jcb.200811067 |
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author | Zaidel-Bar, Ronen |
author_facet | Zaidel-Bar, Ronen |
author_sort | Zaidel-Bar, Ronen |
collection | PubMed |
description | Integrin-mediated adhesion is as ancient as multicellularity, but it was not always as complex as it is in humans. Here, I examine the extent of conservation of 192 adhesome proteins across the genomes of nine model organisms spanning one and a half billion years of evolution. The work reveals that Rho GTPases, lipid- and serine/threonine-kinases, and phosphatases existed before integrins, but tyrosine phosphorylation developed concomitant with integrins. The expansion of specific functional groups such as GAPs, GEFs, adaptors, and receptors is demonstrated, along with the expansion of specific protein domains, such as SH3, PH, SH2, CH, and LIM. Expansion is due to gene duplication and creation of families of paralogues. Apparently, these paralogues share few partners and create new sets of interactions, thus increasing specificity and the repertoire of integrin-mediated signaling. Interestingly, the average number of interactions positively correlates with the evolutionary age of proteins. While shedding light on the evolution of adhesome complexity, this analysis also highlights the relevance and creates a framework for studying integrin-mediated adhesion in simpler model organisms. |
format | Text |
id | pubmed-2728394 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-27283942010-02-10 Evolution of complexity in the integrin adhesome Zaidel-Bar, Ronen J Cell Biol Reviews Integrin-mediated adhesion is as ancient as multicellularity, but it was not always as complex as it is in humans. Here, I examine the extent of conservation of 192 adhesome proteins across the genomes of nine model organisms spanning one and a half billion years of evolution. The work reveals that Rho GTPases, lipid- and serine/threonine-kinases, and phosphatases existed before integrins, but tyrosine phosphorylation developed concomitant with integrins. The expansion of specific functional groups such as GAPs, GEFs, adaptors, and receptors is demonstrated, along with the expansion of specific protein domains, such as SH3, PH, SH2, CH, and LIM. Expansion is due to gene duplication and creation of families of paralogues. Apparently, these paralogues share few partners and create new sets of interactions, thus increasing specificity and the repertoire of integrin-mediated signaling. Interestingly, the average number of interactions positively correlates with the evolutionary age of proteins. While shedding light on the evolution of adhesome complexity, this analysis also highlights the relevance and creates a framework for studying integrin-mediated adhesion in simpler model organisms. The Rockefeller University Press 2009-08-10 /pmc/articles/PMC2728394/ /pubmed/19667126 http://dx.doi.org/10.1083/jcb.200811067 Text en © 2009 Zaidel-Bar This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Reviews Zaidel-Bar, Ronen Evolution of complexity in the integrin adhesome |
title | Evolution of complexity in the integrin adhesome |
title_full | Evolution of complexity in the integrin adhesome |
title_fullStr | Evolution of complexity in the integrin adhesome |
title_full_unstemmed | Evolution of complexity in the integrin adhesome |
title_short | Evolution of complexity in the integrin adhesome |
title_sort | evolution of complexity in the integrin adhesome |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2728394/ https://www.ncbi.nlm.nih.gov/pubmed/19667126 http://dx.doi.org/10.1083/jcb.200811067 |
work_keys_str_mv | AT zaidelbarronen evolutionofcomplexityintheintegrinadhesome |