Tyrosine phosphorylation controls PCNA function through protein stability

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Title:	Tyrosine phosphorylation controls PCNA function through protein stability
Authors:	(Shao-Chun Wang);(Yusuke Nakajima);余永倫(Yung-Luen Yu);(Weiya Xia);(Chun-Te Chen);(Cheng-Chieh Yang);(Eric W. McIntush);李龍緣(Long-Yuan Li);(David H. Hawke);(Ryuji Kobayashi);洪明奇(Mien-Chie Hung)*
Contributors:	醫學院癌症生物學研究所;中國附醫院長室
Date:	2006-12
Issue Date:	2009-08-26 16:11:30 (UTC+8)
Abstract:	The proliferating cell nuclear antigen (PCNA) is an essential protein for DNA replication and damage repair. How its function is controlled remains an important question. Here, we show that the chromatin-bound PCNA protein is phosphorylated on Tyr 211, which is required for maintaining its function on chromatin and is dependent on the tyrosine kinase activity of EGF receptor (EGFR) in the nucleus. Phosphorylation on Tyr 211 by EGFR stabilizes chromatin-bound PCNA protein and associated functions. Consistently, increased PCNA Tyr 211 phosphorylation coincides with pronounced cell proliferation, and is better correlated with poor survival of breast cancer patients, as well as nuclear EGFR in tumours, than is the total PCNA level. These results identify a novel nuclear mechanism linking tyrosine kinase receptor function with the regulation of the PCNA sliding clamp.
Relation:	NATURE CELL BIOLOGY 12(8)1359 ~1368
Appears in Collections:	[Graduate Institute of Cancer Biology] Journal articles

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