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Originally published In Press as doi:10.1074/jbc.M000445200 on March 31, 2000
J. Biol. Chem., Vol. 275, Issue 23, 17412-17419, June 9, 2000
TREK-2, a New Member of the Mechanosensitive Tandem-pore
K+ Channel Family*
Hyoweon
Bang ,
Yangmi
Kim, and
Donghee
Kim§
From the Department of Physiology and Biophysics, Finch University
of Health Sciences/The Chicago Medical School,
North Chicago, Illinois 60064
Recently, several mammalian K+
channel subunits (TWIK, TREK-1, TRAAK, and TASK) possessing four
transmembrane segments and two pore-forming domains have been
identified. We report the cloning of a new member of this tandem-pore
K+ channel from a rat cerebellum cDNA library. It is a
538-amino acid protein and shares 65% amino acid sequence identity
with TREK-1. Therefore, the new clone was named TREK-2. Unlike TREK-1, whose mRNA has been reported to be expressed in many different tissues, TREK-2 mRNA is expressed mainly in the cerebellum, spleen, and testis as judged by reverse transcriptase-polymerase chain reaction
and Northern blot analysis. Expression of TREK-2 in COS-7 cells induced
a time-independent and non-inactivating K+-selective
current. TREK-2 was partially blocked (36%) by 2 mM Ba2+. In symmetrical 150 mM KCl, the
single-channel conductances were 110 picosiemens at 40 mV and 68 picosiemens at +40 mV, and the mean open time was 0.9 ms at 40 mV.
TREK-2 was activated by membrane stretch or acidic pH. At 40 mm Hg
pressure, channel activity increased 10-fold above the basal level.
TREK-2 was also activated by arachidonic acid and other naturally
occurring unsaturated free fatty acids. These results show that TREK-2
is a new member of the tandem-pore K+ channel family and
belongs to the class of mechanosensitive and fatty acid-stimulated
K+ channels.
*
This work was supported by a grant-in-aid from the American
Heart Association.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF196965.
Present address: Dept. of Physiology, Chung-Ang University College
of Medicine, Seoul 156-756, Korea.
§
To whom correspondence should be addressed: Dept. of Physiology and
Biophysics, Finch University of Health Sciences/The Chicago Medical
School, 3333 Green Bay Rd., North Chicago, IL 60064. Tel.: 847-578-3280; Fax: 847-578-3265; E-mail:
donghee.kim@finchcms.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
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