期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 277, 期 8, 页码 6088-6096出版社
ELSEVIER
DOI: 10.1074/jbc.M104851200
关键词
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G protein-sensitive inwardly rectifying potassium (GIRK) channels are activated through direct interactions of their cytoplasmic N- and C-terminal domains with the betagamma subunits of G proteins. By using a combination of biochemical and electrophysiological approaches, we identified minimal N- and C-terminal Gbetagamma-binding domains responsible for stimulation of GIRK4 channel activity. Within these domains one N-terminal residue, His-64, and one C-terminal residue, Leu-268, proved critical for Gbetagamma-mediated GIRK4 activity. Moreover, mutations at these GIRK4 sites reduced significantly binding of the channel domains to Goy. The corresponding residues in GIRK1 also showed a critical involvement in Gbetagamma sensitivity. In GIRK4/GIRK1 heteromers the GIRK4 His-64 and Leu-268 residues showed greater contributions to Goy sensitivity than did the corresponding GIRK1 His-57 and Leu-262 residues. These results identify functionally important channel interaction sites with the betagamma subunits of G proteins, critical for channel activity.
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