Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autor principal: Zaidel-Bar, Ronen
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2009
Materias:
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
_version_ 1782170732077252608
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