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Originally published In Press as doi:10.1074/jbc.M910205199 on March 21, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16697-16701, June 2, 2000
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Identification of the Cystic Fibrosis Transmembrane Conductance Regulator Domains That Are Important for Interactions with ROMK2*

Paula CahillDagger , Malcolm W. Nason Jr.Dagger , Catherine AmbroseDagger , Tong-Yi YaoDagger , Pamela Thomas§, and Marie E. EganDagger

From the Dagger  Department of Pediatrics, Yale University School of Medicine, New Haven, Connecticutt 06520-8026 and the § University of Michigan, Department of Pediatrics, MSRB III, Ann Arbor, Michigan 48109-0646

In addition to functioning as a cAMP-activated chloride channel, the cystic fibrosis transmembrane conductance regulator (CFTR) plays an important role in conferring regulatory properties on other ion channels. It is known, with respect to CFTR regulation of ROMK2 (renally derived KATP channel), that the first transmembrane domain and the first nucleotide binding fold domain (NBF1) of CFTR are necessary for this interaction to occur. It has been shown that under conditions that promote phosphorylation, the ROMK2-CFTR interaction is attenuated. To elucidate the complex nature of this interaction, CFTR constructs were co-expressed with ROMK2 in Xenopus oocytes, and two microelectrode voltage clamp experiments were performed. Although the second half of CFTR can act as a functional chloride channel, our results suggest that it does not confer glibenclamide sensitivity on ROMK2, as does the first half of CFTR. The attenuation of the ROMK2-CFTR interaction under conditions that promote phosphorylation is dependent on at least the presence of the R domain of CFTR. We conclude that transmembrane domain 1, NBF1, and the R domain are the CFTR domains involved in the ROMK2-CFTR interaction and that NBF2 and transmembrane domain 2 are not essential. Lastly, the R domain of CFTR is necessary for the attenuation of the ROMK2-CFTR interaction under conditions that promote phosphorylation.

* This work was supported by Grants HL-03023 and DK-53428 from the National Institutes of Health (to M. E. E.).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: Dept. of Pediatrics, Div. of Respiratory Medicine, Yale University School of Medicine, Fitkin Rm. 503, New Haven, CT 06520-8026. Tel.: 203-785-2480; Fax: 203-785-6337; E-mail: marie.egan@yale.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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