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Proteomic analysis of a eukaryotic cilium
Cilia and flagella are widespread cell organelles that have been highly conserved throughout evolution and play important roles in motility, sensory perception, and the life cycles of eukaryotes ranging from protists to humans. Despite the ubiquity and importance of these organelles, their compositi...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2005
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171396/ https://www.ncbi.nlm.nih.gov/pubmed/15998802 http://dx.doi.org/10.1083/jcb.200504008 |
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author | Pazour, Gregory J. Agrin, Nathan Leszyk, John Witman, George B. |
author_facet | Pazour, Gregory J. Agrin, Nathan Leszyk, John Witman, George B. |
author_sort | Pazour, Gregory J. |
collection | PubMed |
description | Cilia and flagella are widespread cell organelles that have been highly conserved throughout evolution and play important roles in motility, sensory perception, and the life cycles of eukaryotes ranging from protists to humans. Despite the ubiquity and importance of these organelles, their composition is not well known. Here we use mass spectrometry to identify proteins in purified flagella from the green alga Chlamydomonas reinhardtii. 360 proteins were identified with high confidence, and 292 more with moderate confidence. 97 out of 101 previously known flagellar proteins were found, indicating that this is a very complete dataset. The flagellar proteome is rich in motor and signal transduction components, and contains numerous proteins with homologues associated with diseases such as cystic kidney disease, male sterility, and hydrocephalus in humans and model vertebrates. The flagellum also contains many proteins that are conserved in humans but have not been previously characterized in any organism. The results indicate that flagella are far more complex than previously estimated. |
format | Text |
id | pubmed-2171396 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21713962008-03-05 Proteomic analysis of a eukaryotic cilium Pazour, Gregory J. Agrin, Nathan Leszyk, John Witman, George B. J Cell Biol Research Articles Cilia and flagella are widespread cell organelles that have been highly conserved throughout evolution and play important roles in motility, sensory perception, and the life cycles of eukaryotes ranging from protists to humans. Despite the ubiquity and importance of these organelles, their composition is not well known. Here we use mass spectrometry to identify proteins in purified flagella from the green alga Chlamydomonas reinhardtii. 360 proteins were identified with high confidence, and 292 more with moderate confidence. 97 out of 101 previously known flagellar proteins were found, indicating that this is a very complete dataset. The flagellar proteome is rich in motor and signal transduction components, and contains numerous proteins with homologues associated with diseases such as cystic kidney disease, male sterility, and hydrocephalus in humans and model vertebrates. The flagellum also contains many proteins that are conserved in humans but have not been previously characterized in any organism. The results indicate that flagella are far more complex than previously estimated. The Rockefeller University Press 2005-07-04 /pmc/articles/PMC2171396/ /pubmed/15998802 http://dx.doi.org/10.1083/jcb.200504008 Text en Copyright © 2005, The Rockefeller University Press 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.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Pazour, Gregory J. Agrin, Nathan Leszyk, John Witman, George B. Proteomic analysis of a eukaryotic cilium |
title | Proteomic analysis of a eukaryotic cilium |
title_full | Proteomic analysis of a eukaryotic cilium |
title_fullStr | Proteomic analysis of a eukaryotic cilium |
title_full_unstemmed | Proteomic analysis of a eukaryotic cilium |
title_short | Proteomic analysis of a eukaryotic cilium |
title_sort | proteomic analysis of a eukaryotic cilium |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171396/ https://www.ncbi.nlm.nih.gov/pubmed/15998802 http://dx.doi.org/10.1083/jcb.200504008 |
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