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J Biol Chem, Vol. 274, Issue 12, 7887-7892, March 19, 1999
From Potassium channels are found in all mammalian
cell types, and they perform many distinct functions in both excitable
and non-excitable cells. These functions are subserved by several
different families of potassium channels distinguishable by primary
sequence features as well as by physiological characteristics. Of these
families, the tandem pore domain potassium channels are a new and
distinct class, primarily distinguished by the presence of two
pore-forming domains within a single polypeptide chain. We have cloned
a new member of this family, TWIK-2, from a human brain cDNA
library. Primary sequence analysis of TWIK-2 shows that it is most
closely related to TWIK-1, especially in the pore-forming domains.
Northern blot analysis reveals the expression of TWIK-2 in all human
tissues assayed except skeletal muscle. Human TWIK-2 expressed
heterologously in Xenopus oocytes is a non-inactivating
weak inward rectifier with channel properties similar to TWIK-1.
Pharmacologically, TWIK-2 channels are distinct from TWIK-1 channels in
their response to quinidine, quinine, and barium. TWIK-2 is inhibited
by intracellular, but not extracellular, acidification. This new clone
reveals the existence of a subfamily in the tandem pore domain
potassium channel family with weak inward rectification properties.
TWIK-2, a New Weak Inward Rectifying Member of the Tandem
Pore Domain Potassium Channel Family
,,, and Elan Pharmaceuticals,
Menlo Park, California 94025 and the § Department of
Anesthesia and Perioperative Care, School of Medicine, University of
California, San Francisco, California 94143-0542
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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