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J. Biol. Chem., Vol. 275, Issue 41, 32027-32036, October 13, 2000
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From the Groupe de Recherche en Néphrologie,
To date, the cation-Cl The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF284422.
Cloning and Functional Characterization of a
Cation-Cl
Cotransporter-interacting Protein*
,, and
Department of Medicine, and the Unité de Recherche
en Génétique Humaine et Moléculaire,
§ Department of Medical Biology, Faculty of Medicine, Laval
University, Québec G1R 2J6, Canada
cotransporter (CCC) family comprises two branches of homologous
membrane proteins. One branch includes the
Na+-K+-Cl cotransporters (NKCCs)
and the Na+-Cl cotransporter, and the other
branch includes the K+-Cl cotransporters.
Here, we have isolated the first member of a third CCC family branch.
This member shares ~25% identity in amino acid sequence with each of
the other known mammalian CCCs. The corresponding cDNA, obtained
from a human heart library and initially termed WO3.3,
encodes a 914-residue polypeptide of 96.2 kDa (calculated mass).
Sequence analyses predict a 12-transmembrane domain (tm) region, two
N-linked glycosylation sites between tm5 and
tm6, and a large intracellular carboxyl terminus containing
protein kinase C phosphorylation sites. Northern blot analysis uncovers an ~3.7-kilobase pair transcript present in muscle, placenta, brain,
and kidney. With regard to function, WO3.3 expressed either in HEK-293 cells or Xenopus laevis oocytes does not
increase Rb+-, Na+-, and
Cl-coupled transport during 5- or 6-h fluxes,
respectively. In the oocyte, however, WO3.3 specifically
inhibits human NKCC1-mediated 86Rb+ flux. In
addition, coimmunoprecipitation studies using lysates from
WO3.3-transfected HEK-293 cells suggest a direct
interaction of WO3.3 with endogenous NKCC. Thus, we have
cloned and characterized the first putative heterologous
CCC-interacting protein (CIP) known at present. CIP1 may be part of a
novel family of proteins that modifies the activity or kinetics of CCCs
through heterodimer formation.
*
This work was supported by grants from the Medical Research
Council of Canada (characterization of hCIP1), the Heart & Stroke Foundation of Canada (production of anti-C1), and the Kidney Foundation of Canada (studies on NKCC2).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.
Medical Research Council Clinician Scientist II. To whom
correspondence should be addressed: Research Center L'Hôtel-Dieu de Québec of the CHUQ, 10 Rue McMahon, Rm. 3852, Québec
(Qué) G1R2J6, Canada. Tel.: 418-691-5477; Fax: 418-691-5787;
E-mail: paul.isenring@crhdq.ulaval.ca.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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