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Molecular and Cellular Biology, October 2005, p. 8619-8630, Vol. 25, No. 19
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.19.8619-8630.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

JAMP, a Jun N-Terminal Kinase 1 (JNK1)-Associated Membrane Protein, Regulates Duration of JNK Activity

Takayuki Kadoya,^2, Ashwani Khurana,^1, Marianna Tcherpakov,¹ Kenneth D. Bromberg,² Christine Didier,² Limor Broday,² Toshimasa Asahara,³ Anindita Bhoumik,¹ and Ze'ev Ronai^1*

Signal Transduction Program, The Burnham Institute, La Jolla, California,¹ Department of Oncological Sciences, Mount Sinai School of Medicine, New York, New York 10029,² Department of Surgery, Hiroshima University, Hiroshima 734-8551, Japan³

Received 5 April 2005/ Returned for modification 6 May 2005/ Accepted 8 July 2005

We report the identification and characterization of JAMP (JNK1 [Jun N-terminal kinase 1]-associated membrane protein), a predicted seven-transmembrane protein that is localized primarily within the plasma membrane and associates with JNK1 through its C-terminal domain. JAMP association with JNK1 outcompetes JNK1 association with mitogen-activated protein kinase phosphatase 5, resulting in increased and prolonged JNK1 activity following stress. Elevated expression of JAMP following UV or tunicamycin treatment results in sustained JNK activity and a higher level of JNK-dependent apoptosis. Inhibition of JAMP expression by RNA interference reduces the degree and duration of JNK activation and concomitantly the level of stress-induced apoptosis. Through its regulation of JNK1 activity, JAMP emerges as a membrane-anchored regulator of the duration of JNK1 activity in response to diverse stress stimuli.

Supplemental material for this article may be found at http://mcb.asm.org/.

These authors contributed equally to this work.