JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein, regulates duration of JNK activity.
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.
Mesh Terms:
3T3 Cells, Amino Acid Sequence, Animals, Apoptosis, Carrier Proteins, Cell Line, Cell Line, Tumor, Cell Membrane, Cell Movement, DNA, DNA, Complementary, Dual-Specificity Phosphatases, Gene Expression Regulation, Enzymologic, Glycosylation, Green Fluorescent Proteins, HeLa Cells, Humans, Immunoprecipitation, MAP Kinase Signaling System, Membrane Glycoproteins, Mice, Microscopy, Confocal, Molecular Sequence Data, NIH 3T3 Cells, Phosphoprotein Phosphatases, Protein Binding, Protein Structure, Tertiary, RNA Interference, Reverse Transcriptase Polymerase Chain Reaction, Subcellular Fractions, Time Factors, Tissue Distribution, Transfection, Tunicamycin, Ultraviolet Rays
3T3 Cells, Amino Acid Sequence, Animals, Apoptosis, Carrier Proteins, Cell Line, Cell Line, Tumor, Cell Membrane, Cell Movement, DNA, DNA, Complementary, Dual-Specificity Phosphatases, Gene Expression Regulation, Enzymologic, Glycosylation, Green Fluorescent Proteins, HeLa Cells, Humans, Immunoprecipitation, MAP Kinase Signaling System, Membrane Glycoproteins, Mice, Microscopy, Confocal, Molecular Sequence Data, NIH 3T3 Cells, Phosphoprotein Phosphatases, Protein Binding, Protein Structure, Tertiary, RNA Interference, Reverse Transcriptase Polymerase Chain Reaction, Subcellular Fractions, Time Factors, Tissue Distribution, Transfection, Tunicamycin, Ultraviolet Rays
Mol. Cell. Biol.
Date: Oct. 01, 2005
PubMed ID: 16166642
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