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MBC in Press, published online ahead of print July 11, 2007
Mol. Biol. Cell 10.1091/mbc.E06-07-0604

A more recent version of this article appeared on September 1, 2007
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Submitted on July 17, 2006
Revised on June 12, 2007
Accepted on June 29, 2007

Chromatin Remodeling Proteins Interact with Pericentrin to Regulate Centrosome Integrity

James Edward Sillibourne,* Bénédicte Delaval, Sambra Redick, Manisha Sinah, and Stephen John Doxsey

Program in Molecular Medicine, University of Massachusetts, Worcester, MA 01605

Monitoring Editor: Tim Stearns

Pericentrin is an integral centrosomal component that anchors regulatory and structural molecules to centrosomes. In a yeast two-hybrid screen with pericentrin we identified chromodomain helicase DNA-binding protein 4 (CHD4/Mi2{beta}). CHD4 is part of the multi-protein nucleosome remodelling deacetylase (NuRD) complex. We show that many NuRD components interacted with pericentrin by coimmunoprecipitation and that they localized to centrosomes and midbodies. Overexpression of the pericentrin-binding domain of CHD4 or another family member (CHD3) dissociated pericentrin from centrosomes. Depletion of CHD3, but not CHD4, by RNA interference dissociated pericentrin and {gamma}-tubulin from centrosomes. Microtubule nucleation/organization, cell morphology and nuclear centration were disrupted in CHD3-depleted cells. Spindles were disorganized, the majority showing a prometaphase-like configuration. Time-lapse imaging revealed mitotic failure before chromosome segregation and cytokinesis failure. We conclude that pericentrin forms complexes with CHD3 and CHD4, but a distinct CHD3-pericentrin complex is required for centrosomal anchoring of pericentrin/{gamma}-tubulin and for centrosome integrity.

*Present address: Institut Curie, Section Recherche UMR 144 du CNRS, 26 Rue d’Ulm, Paris 75248, France.

Address correspondence to: Stephen John Doxsey (stephen.doxsey{at}umassmed.edu)




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