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J. Biol. Chem., Vol. 277, Issue 41, 38272-38283, October 11, 2002
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From the A novel human connexin gene (GJA11)
was cloned from a genomic library. The open reading frame encoded a
hypothetical protein of 294 amino acid residues with a predicted
molecular mass of 31,933, hence referred to as connexin-31.9 (Cx31.9)
or The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY093445 (partial sequence of the connexin-31.9 gene).
Molecular Cloning, Functional Expression, and Tissue Distribution
of a Novel Human Gap Junction-forming Protein, Connexin-31.9
INTERACTION WITH ZONA OCCLUDENS PROTEIN-1*
§,
,,§§
Department of Cell Biology, Scripps Research
Institute, La Jolla, California 92037, the ¶ Department of
Physiology and Biophysics, University of California, Irvine, California
92697, and the ** Division of Cellular Biochemistry,
Netherlands Cancer Institute,
1066 CX Amsterdam, The Netherlands
11 connexin. A clone in GenBankTM containing the
Cx31.9 gene localized to chromosome 17q21.2. Northern analysis of Cx31.9 showed a major 4.4-kilobase transcript,
which was expressed at varying levels in all tissues analyzed. Two
monoclonal antibodies generated against different domains of Cx31.9
recognized a 30-33-kDa protein from cells overexpressing Cx31.9.
Immunofluorescence of overexpressing cells indicated the presence of
Cx31.9 between adjacent cells, consistent with its localization to gap
junctions. Double voltage clamp analyses of Cx31.9-overexpressing
cells, and of paired Xenopus oocytes injected with Cx31.9
cRNA, demonstrated junctional currents indicative of gap junction
channel formation. In contrast to previously characterized connexins,
Cx31.9 showed no voltage-dependent gating within a
physiologically relevant range. Cx31.9 was detected in human tissues by
immunoblot analysis, and immunofluorescence localized Cx31.9 expression
to vascular smooth muscle cells. Furthermore, it was demonstrated that
Cx31.9 interacted with ZO-1. Thus, Cx31.9 represents a novel connexin gene that in vivo generates a protein with unique
voltage gating properties.
*
This work was supported by a grant from the Danish Research
Council (to P. A. N.) and by National Institutes of Health
Grant EY12142 (to N. M. K.).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.
Present address: Dept. of Biological Sciences, State
University of New York, Buffalo, NY 14260.
Present address: Celera Genomics, South San Francisco, CA 94080.
§§
To whom correspondence may be addressed. Present address: Dept.
of Ophthalmology and Visual Sciences (MC 649), University of Illinois,
1905 W. Taylor St., Chicago, IL 60612-7243. Tel.: 312-413-5414; Fax:
312-413-5614; E-mail: nalin@uic.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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