期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 281, 期 31, 页码 21954-21962出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M601578200
关键词
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Mounting evidence suggests that the ion pump, Na, K-ATPase, can, in the presence of ouabain, act as a signal transducer. A prominent binding motif linking the Na, K-ATPase to intracellular signaling effectors has, however, not yet been identified. Here we report that the N-terminal tail of the Na, K-ATPase catalytic alpha-subunit (alpha NT-t) binds directly to the N terminus of the inositol 1,4,5-trisphosphate receptor. Three amino acid residues, LKK, conserved in most species and most alpha-isoforms, are essential for the binding to occur. In wild-type cells, low concentrations of ouabain trigger low frequency calcium oscillations that activate NF-kappa B and protect from apoptosis. All of these effects are suppressed in cells overexpressing a peptide corresponding to alpha NT-t but not in cells overexpressing a peptide corresponding to alpha NT- t Delta LKK. Thus we have identified a well conserved Na, K-ATPase motif that binds to the inositol 1,4,5-trisphosphate receptor and can trigger an anti-apoptotic calcium signal.
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