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Highly diversified expansions shaped the evolution of membrane bound proteins in metazoans
The dramatic increase in membrane proteome complexity is arguably one of the most pivotal evolutionary events that underpins the origin of multicellular animals. However, the origin of a significant number of membrane families involved in metazoan development has not been clarified. In this study, w...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5620054/ https://www.ncbi.nlm.nih.gov/pubmed/28959054 http://dx.doi.org/10.1038/s41598-017-11543-z |
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author | Attwood, Misty M. Krishnan, Arunkumar Almén, Markus Sällman Schiöth, Helgi B. |
author_facet | Attwood, Misty M. Krishnan, Arunkumar Almén, Markus Sällman Schiöth, Helgi B. |
author_sort | Attwood, Misty M. |
collection | PubMed |
description | The dramatic increase in membrane proteome complexity is arguably one of the most pivotal evolutionary events that underpins the origin of multicellular animals. However, the origin of a significant number of membrane families involved in metazoan development has not been clarified. In this study, we have manually curated the membrane proteomes of 22 metazoan and 2 unicellular holozoan species. We identify 123,014 membrane proteins in these 24 eukaryotic species and classify 86% of the dataset. We determine 604 functional clusters that are present from the last holozoan common ancestor (LHCA) through many metazoan species. Intriguingly, we show that more than 70% of the metazoan membrane protein families have a premetazoan origin. The data show that enzymes are more highly represented in the LHCA and expand less than threefold throughout metazoan species; in contrast to receptors that are relatively few in the LHCA but expand nearly eight fold within metazoans. Expansions related to cell adhesion, communication, immune defence, and developmental processes are shown in conjunction with emerging biological systems, such as neuronal development, cytoskeleton organization, and the adaptive immune response. This study defines the possible LHCA membrane proteome and describes the fundamental functional clusters that underlie metazoan diversity and innovation. |
format | Online Article Text |
id | pubmed-5620054 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-56200542017-10-11 Highly diversified expansions shaped the evolution of membrane bound proteins in metazoans Attwood, Misty M. Krishnan, Arunkumar Almén, Markus Sällman Schiöth, Helgi B. Sci Rep Article The dramatic increase in membrane proteome complexity is arguably one of the most pivotal evolutionary events that underpins the origin of multicellular animals. However, the origin of a significant number of membrane families involved in metazoan development has not been clarified. In this study, we have manually curated the membrane proteomes of 22 metazoan and 2 unicellular holozoan species. We identify 123,014 membrane proteins in these 24 eukaryotic species and classify 86% of the dataset. We determine 604 functional clusters that are present from the last holozoan common ancestor (LHCA) through many metazoan species. Intriguingly, we show that more than 70% of the metazoan membrane protein families have a premetazoan origin. The data show that enzymes are more highly represented in the LHCA and expand less than threefold throughout metazoan species; in contrast to receptors that are relatively few in the LHCA but expand nearly eight fold within metazoans. Expansions related to cell adhesion, communication, immune defence, and developmental processes are shown in conjunction with emerging biological systems, such as neuronal development, cytoskeleton organization, and the adaptive immune response. This study defines the possible LHCA membrane proteome and describes the fundamental functional clusters that underlie metazoan diversity and innovation. Nature Publishing Group UK 2017-09-28 /pmc/articles/PMC5620054/ /pubmed/28959054 http://dx.doi.org/10.1038/s41598-017-11543-z Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Attwood, Misty M. Krishnan, Arunkumar Almén, Markus Sällman Schiöth, Helgi B. Highly diversified expansions shaped the evolution of membrane bound proteins in metazoans |
title | Highly diversified expansions shaped the evolution of membrane bound proteins in metazoans |
title_full | Highly diversified expansions shaped the evolution of membrane bound proteins in metazoans |
title_fullStr | Highly diversified expansions shaped the evolution of membrane bound proteins in metazoans |
title_full_unstemmed | Highly diversified expansions shaped the evolution of membrane bound proteins in metazoans |
title_short | Highly diversified expansions shaped the evolution of membrane bound proteins in metazoans |
title_sort | highly diversified expansions shaped the evolution of membrane bound proteins in metazoans |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5620054/ https://www.ncbi.nlm.nih.gov/pubmed/28959054 http://dx.doi.org/10.1038/s41598-017-11543-z |
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