Functional divergence and evolutionary turnover in mammalian phosphoproteomes.

Protein phosphorylation is a key mechanism to regulate protein functions. However, the contribution of this protein modification to species divergence is still largely unknown. Here, we studied the evolution of mammalian phosphoregulation by comparing the human and mouse phosphoproteomes. We found t...

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Autores principales:	Luca Freschi, Mazid Osseni, Christian R Landry
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Genetics QH426-470
Acceso en línea:	https://doaj.org/article/2481df05c39e4db4a52a212d5ce5896b
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spelling	oai:doaj.org-article:2481df05c39e4db4a52a212d5ce5896b2021-11-18T06:21:17ZFunctional divergence and evolutionary turnover in mammalian phosphoproteomes.1553-73901553-740410.1371/journal.pgen.1004062https://doaj.org/article/2481df05c39e4db4a52a212d5ce5896b2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24465218/?tool=EBIhttps://doaj.org/toc/1553-7390https://doaj.org/toc/1553-7404Protein phosphorylation is a key mechanism to regulate protein functions. However, the contribution of this protein modification to species divergence is still largely unknown. Here, we studied the evolution of mammalian phosphoregulation by comparing the human and mouse phosphoproteomes. We found that 84% of the positions that are phosphorylated in one species or the other are conserved at the residue level. Twenty percent of these conserved sites are phosphorylated in both species. This proportion is 2.5 times more than expected by chance alone, suggesting that purifying selection is preserving phosphoregulation. However, we show that the majority of the sites that are conserved at the residue level are differentially phosphorylated between species. These sites likely result from false-negative identifications due to incomplete experimental coverage, false-positive identifications and non-functional sites. In addition, our results suggest that at least 5% of them are likely to be true differentially phosphorylated sites and may thus contribute to the divergence in phosphorylation networks between mouse and humans and this, despite residue conservation between orthologous proteins. We also showed that evolutionary turnover of phosphosites at adjacent positions (in a distance range of up to 40 amino acids) in human or mouse leads to an over estimation of the divergence in phosphoregulation between these two species. These sites tend to be phosphorylated by the same kinases, supporting the hypothesis that they are functionally redundant. Our results support the hypothesis that the evolutionary turnover of phosphorylation sites contributes to the divergence in phosphorylation profiles while preserving phosphoregulation. Overall, our study provides advanced analyses of mammalian phosphoproteomes and a framework for the study of their contribution to phenotypic evolution.Luca FreschiMazid OsseniChristian R LandryPublic Library of Science (PLoS)articleGeneticsQH426-470ENPLoS Genetics, Vol 10, Iss 1, p e1004062 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Genetics QH426-470
spellingShingle	Genetics QH426-470 Luca Freschi Mazid Osseni Christian R Landry Functional divergence and evolutionary turnover in mammalian phosphoproteomes.
description	Protein phosphorylation is a key mechanism to regulate protein functions. However, the contribution of this protein modification to species divergence is still largely unknown. Here, we studied the evolution of mammalian phosphoregulation by comparing the human and mouse phosphoproteomes. We found that 84% of the positions that are phosphorylated in one species or the other are conserved at the residue level. Twenty percent of these conserved sites are phosphorylated in both species. This proportion is 2.5 times more than expected by chance alone, suggesting that purifying selection is preserving phosphoregulation. However, we show that the majority of the sites that are conserved at the residue level are differentially phosphorylated between species. These sites likely result from false-negative identifications due to incomplete experimental coverage, false-positive identifications and non-functional sites. In addition, our results suggest that at least 5% of them are likely to be true differentially phosphorylated sites and may thus contribute to the divergence in phosphorylation networks between mouse and humans and this, despite residue conservation between orthologous proteins. We also showed that evolutionary turnover of phosphosites at adjacent positions (in a distance range of up to 40 amino acids) in human or mouse leads to an over estimation of the divergence in phosphoregulation between these two species. These sites tend to be phosphorylated by the same kinases, supporting the hypothesis that they are functionally redundant. Our results support the hypothesis that the evolutionary turnover of phosphorylation sites contributes to the divergence in phosphorylation profiles while preserving phosphoregulation. Overall, our study provides advanced analyses of mammalian phosphoproteomes and a framework for the study of their contribution to phenotypic evolution.
format	article
author	Luca Freschi Mazid Osseni Christian R Landry
author_facet	Luca Freschi Mazid Osseni Christian R Landry
author_sort	Luca Freschi
title	Functional divergence and evolutionary turnover in mammalian phosphoproteomes.
title_short	Functional divergence and evolutionary turnover in mammalian phosphoproteomes.
title_full	Functional divergence and evolutionary turnover in mammalian phosphoproteomes.
title_fullStr	Functional divergence and evolutionary turnover in mammalian phosphoproteomes.
title_full_unstemmed	Functional divergence and evolutionary turnover in mammalian phosphoproteomes.
title_sort	functional divergence and evolutionary turnover in mammalian phosphoproteomes.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/2481df05c39e4db4a52a212d5ce5896b
work_keys_str_mv	AT lucafreschi functionaldivergenceandevolutionaryturnoverinmammalianphosphoproteomes AT mazidosseni functionaldivergenceandevolutionaryturnoverinmammalianphosphoproteomes AT christianrlandry functionaldivergenceandevolutionaryturnoverinmammalianphosphoproteomes
_version_	1718424465538285568

Functional divergence and evolutionary turnover in mammalian phosphoproteomes.

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