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First published online 13 December 2005
doi: 10.1242/jcs.02699

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Nuclear protein NP60 regulates p38 MAPK activity

Jing Fu^1,*, Ziqiang Yang^1,*, Jinxue Wei¹, Jiahuai Han² and Jun Gu^1,

¹ National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, People's Republic of China
² Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA

Author for correspondence (e-mail: gj{at}pku.edu.cn)

Accepted 19 September 2005

The activation of p38 is mediated by its upstream kinase and associated proteins. Here we identify a new nuclear protein, NP60, which regulates the activation of p38 in response to sorbitol treatment. NP60 specifically binds to p38, but not to JNK and ERK, in vitro and in vivo. Co-transfection of NP60 leads to the phosphorylation and activation of p38, and subsequently results in the phosphorylation and activation of activating transcription factor 2. The phosphorylation of p38 induced by NP60 requires upstream activity of p38 MAP kinase, MAP kinase kinase 6 (MKK6) or MKK4. Our results indicate that NP60 mediates stress activation of p38 and regulates p38 signaling in a specific way.

Key words: NP60, p38 phosphorylation, Signaling, Sorbitol