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J. Biol. Chem., Vol. 275, Issue 37, 28757-28763, September 15, 2000
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From the Laboratory of Biochemistry, Division of Applied Life
Sciences, Kyoto University Graduate School of Agriculture,
Kyoto 606-8502, Japan
ATP-sensitive potassium (KATP)
channels, composed of sulfonylurea receptor (SURx) and Kir6.x, play
important roles by linking cellular metabolic state to membrane
potential in various tissues. Pancreatic, cardiac, and vascular smooth
muscle KATP channels, which consist of different subtypes
of SURx, differ in their responses to cellular metabolic state. To
explore the possibility that different interactions of SURx with
nucleotides cause differential regulation of KATP channels,
we analyzed the properties of nucleotide-binding folds (NBFs) of SUR1,
SUR2A, and SUR2B. SURx in crude membrane fractions was incubated with
8-azido-[
Different Binding Properties and Affinities for ATP and ADP among
Sulfonylurea Receptor Subtypes, SUR1, SUR2A, and SUR2B*
-32P]ATP or
8-azido-[
-32P]ATP under various conditions and was
photoaffinity-labeled. Then, SURx was digested mildly with trypsin, and
partial tryptic fragments were immunoprecipitated with antibodies
against NBF1 and NBF2. Some nucleotide-binding properties were
different among SUR subtypes as follows. 1) Mg2+ dependence
of nucleotide binding of NBF2 of SUR1 was high, whereas those of SUR2A
and SUR2B were low. 2) The affinities of NBF1 of SUR1 for ATP and ADP,
especially for ATP, were significantly higher than those of SUR2A and
SUR2B. 3) The affinities of NBF2 of SUR2B for ATP and ADP were
significantly higher than those of SUR2A. This is the first biochemical
study to analyze and compare the nucleotide-binding properties of NBFs
of three SUR subtypes, and our results suggest that their different
properties may explain, in part, the differential regulation of
KATP channel subtypes. The high nucleotide-binding
affinities of SUR1 may explain the high ability of SUR1 to stimulate
pancreatic KATP channels. It is also suggested that the
C-terminal 42 amino acids affect the physiological roles of SUR2A and
SUR2B by changing the nucleotide-binding properties of their NBFs.
*
This work was supported by Grants-in-aid for Scientific
Research on Priority Areas "ABC Proteins" 10217205 from the
Ministry of Education, Science, Sports, and Culture of Japan and by
Research Fellowships of the Japan Society for the Promotion of Science for Young Scientists.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.
To whom correspondence should be addressed: Laboratory of
Biochemistry, Division of Applied Life Sciences, Kyoto University Graduate School of Agriculture, Kyoto 606-8502, Japan. Tel.:
81-75-753-6105; Fax: 81-75-753-6104; E-mail:
uedak@kais.kyoto-u.ac.jp.
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