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(Received for publication, December 5, 1994; and in revised form, January 9, 1995) ATP-sensitive K
Volume 270,
Number 11,
Issue of March 17, 1995 pp. 5691-5694
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
(K
)
channels play a crucial role in coupling metabolic energy to the
membrane potential of cells. We have isolated a cDNA encoding a novel
member (uK-1) of the inward rectifier K channel family from a rat pancreatic islet cDNA library. Rat
uK-1 is a 424-amino acid residue protein (M
= 47,960). Electrophysiological studies
of uK-1 expressed in Xenopus laevis oocytes show
that uK-1 is a weak rectifier and is blocked with
Ba
ions. Single-channel patch clamp study of clonal
human kidney epithelial cells (HEK293) transfected with
uK-1 cDNA reveals that uK-1 closes in
response to 1 mM ATP and has a single channel conductance of
70 ± 2 picosiemens (n = 6), indicating that
uK-1 is an ATP-sensitive inward rectifier
K channel. In addition, uK-1 is
activated by the K channel opener, diazoxide. RNA blot
analysis shows that uK-1 mRNA is expressed ubiquitously
in rat tissues, including pancreatic islets, pituitary, skeletal
muscle, and heart, suggesting that uK-1 may play a
physiological role as a link between the metabolic state and membrane
K permeability of cells in almost every normal tissue.
Since uK-1 shares only 43-46% amino acid identity
with members of previously reported inward rectifier K channel subfamilies, including ROMK1, IRK1, GIRK1, and
cK-1, uK-1 is not an isoform of these
subfamilies and, therefore, represents a new subfamily of the inward
rectifier K channel family having two transmembrane
segments.
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