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Published online
doi:10.1083/jcb.200905031
The Journal of Cell Biology, Vol. 187, No. 3, 355-363
The Rockefeller University Press, 0021-9525 $30.00
© Stevens et al.
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Ana3 is a conserved protein required for the structural integrity of centrioles and basal bodies



Naomi R. Stevens1, Jeroen Dobbelaere1, Alan Wainman2, Fanni Gergely3, and Jordan W. Raff1,2

1 The Gurdon Institute, Cambridge CB2 1QN, England, UK
2 Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, England, UK
3 Cancer Research UK Cambridge Research Institute, Cambridge CB2 0RE, England, UK

Correspondence to Jordan W. Raff: jordan.raff{at}path.ox.ac.uk

Recent studies have identified a conserved "core" of proteins that are required for centriole duplication. A small number of additional proteins have recently been identified as potential duplication factors, but it is unclear whether any of these proteins are components of the core duplication machinery. In this study, we investigate the function of one of these proteins, Drosophila melanogaster Ana3. We show that Ana3 is present in centrioles and basal bodies, but its behavior is distinct from that of the core duplication proteins. Most importantly, we find that Ana3 is required for the structural integrity of both centrioles and basal bodies and for centriole cohesion, but it is not essential for centriole duplication. We show that Ana3 has a mammalian homologue, Rotatin, that also localizes to centrioles and basal bodies and appears to be essential for cilia function. Thus, Ana3 defines a conserved family of centriolar proteins and plays an important part in ensuring the structural integrity of centrioles and basal bodies.

Abbreviations used in this paper: Asl, Asterless; Cnn, Centrosomin; D-PLP, Drosophila pericentrin-like protein; MBP, maltose-binding protein; MT, microtubule; PCM, pericentriolar material; Rttn, Rotatin; shRNA, short hairpin RNA; Ubq, ubiquitin; WT, wild type.

© 2009 Stevens et al.
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