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Kadoya, T, Khurana, A, Tcherpakov, M, Bromberg, KD, Didier, C, Broday, L, Asahara, T, Bhoumik, A and Ronai, Z (2005) JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein, regulates duration of JNK activity. Mol. Cell. Biol. 25:8619-30
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.
3T3 Cells; Amino Acid Sequence; Animals; Apoptosis; Carrier Proteins/biosynthesis; Carrier Proteins/physiology; Cell Line; Cell Line, Tumor; Cell Membrane/metabolism; Cell Movement; DNA/metabolism; DNA, Complementary/metabolism; Dual-Specificity Phosphatases; Gene Expression Regulation, Enzymologic; Glycosylation; Green Fluorescent Proteins/metabolism; HeLa Cells; Humans; Immunoprecipitation; MAP Kinase Signaling System; Membrane Glycoproteins/biosynthesis; Membrane Glycoproteins/physiology; Mice; Microscopy, Confocal; Molecular Sequence Data; NIH 3T3 Cells; Phosphoprotein Phosphatases/metabolism; Protein Binding; Protein Structure, Tertiary; RNA Interference; Reverse Transcriptase Polymerase Chain Reaction; Subcellular Fractions/metabolism; Time Factors; Tissue Distribution; Transfection; Tunicamycin/pharmacology; Ultraviolet Rays
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