{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T20:29:09Z","timestamp":1790886549437,"version":"4.1.0"},"reference-count":44,"publisher":"The Company of Biologists","issue":"18","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2009,9,15]]},"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.1242\/jcs.050245","type":"journal-article","created":{"date-parts":[[2009,8,26]],"date-time":"2009-08-26T02:59:28Z","timestamp":1251255568000},"page":"3312-3321","source":"Crossref","is-referenced-by-count":42,"title":["SUMO-dependent regulation of centrin-2"],"prefix":"10.1242","volume":"122","author":[{"given":"Ulf R.","family":"Klein","sequence":"first","affiliation":[{"name":"Department of Cell Biology, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erich A.","family":"Nigg","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany"},{"name":"Biozentrum, University of Basel, Klingelbergstrasse 50\/70, CH-4056 Basel, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2021042423080345600_REF1","doi-asserted-by":"crossref","unstructured":"Anckar, J. and Sistonen, L. 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