JAMP, a JUB N-terminal kinase 1 (JNK1)-associated membrane protein, regulates duration of JNK activity

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)8619-8630
Number of pages12
JournalMolecular and Cellular Biology
Issue number19
StatePublished - Oct 2005
Externally publishedYes


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