Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/24661
Title: Pix proteins and the evolution of centrioles
Authors: Woodland, H. R.
Fry, Andrew M.
First Published: 20-Nov-2008
Publisher: Public Library of Science
Citation: PLoS ONE, 2008, 3 (11)
Abstract: We have made a wide phylogenetic survey of Pix proteins, which are constituents of vertebrate centrioles in most eukaryotes. We have also surveyed the presence and structure of flagella or cilia and centrioles in these organisms, as far as is possible from published information. We find that Pix proteins are present in a vast range of eukaryotes, but not all. Where centrioles are absent so are Pix proteins. If one considers the maintenance of Pix proteins over evolutionary time scales, our analysis would suggest that their key function is to make cilia and flagella, and the same is true of centrioles. Moreover, this survey raises the possibility that Pix proteins are only maintained to make cilia and flagella that undulate, and even then only when they are constructed by transporting ciliary constituents up the cilium using the intraflagellar transport (IFT) system. We also find that Pix proteins have become generally divergent within Ecdysozoa and between this group and other taxa. This correlates with a simplification of centrioles within Ecdysozoa and a loss or divergence of cilia/flagella. Thus Pix proteins act as a weathervane to indicate changes in centriole function, whose core activity is to make cilia and flagella.
DOI Link: 10.1371/journal.pone.0003778
ISSN: 1932-6203
eISSN: 1932-6203
Links: http://hdl.handle.net/2381/24661
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0003778
Type: Journal Article
Rights: Copyright: 2008 Woodland et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Appears in Collections:Published Articles, Dept. of Biochemistry

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