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First published online 25 August 2009
doi: 10.1242/jcs.050245

Journal of Cell Science 122, 3312-3321 (2009)
Published by The Company of Biologists 2009
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Research Article

SUMO-dependent regulation of centrin-2

Ulf R. Klein1,* and Erich A. Nigg1,2

1 Department of Cell Biology, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany
2 Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland

* Author for correspondence (uklein{at}biochem.mpg.de)

Accepted 15 June 2009

Centrins are multifunctional Ca2+-binding proteins that are highly conserved from yeast to humans. Centrin-2 is a core component of the centrosome of higher eukaryotes. In addition, it is present within the nucleus, in which it is part of the xeroderma pigmentosum group C (XPC) complex, which controls nucleotide excision repair (NER). Regulation of the subcellular distribution of centrin-2 has so far remained elusive. Here we show that centrin-2 is a substrate of SUMOylation in vitro and in vivo, and that it is preferentially modified by SUMO2/3. Moreover, we identify the SUMO E3-like ligase human polycomb protein 2 (PC2; also known as hPC2) as essential for centrin-2 modification. Interference with the SUMOylation pathway leads to a striking defect in nuclear localization of centrin-2 and accumulation in the cytoplasm, whereas centrosomal recruitment of centrin-2 is unaffected. Depletion of the XPC protein mimics this situation and we provide evidence that SUMO conjugation of centrin-2 enhances its binding to the XPC protein. These data show that the nucleocytoplasmic shuttling of centrin-2 depends on the SUMO system and indicates that localization of centrin-2 within the nucleus depends on its ability to bind to the XPC protein.

Key words: Centrins, Centrin-2, XPC, SUMO, hPC2, Nucleocytoplasmic shuttling


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