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J Biol Chem, Vol. 273, Issue 21, 12725-12731, May 22, 1998
From the Department of Medicine and Pathophysiology, Osaka
University Medical School, 2-2 Yamada-oka, Suita,
Osaka 565, Japan
The gap junction protein connexin-43 is normally
located at the intercalated discs of cardiac myocytes, and it plays a
critical role in the synchronization of their contraction. The
mechanism by which connexin-43 is localized within cardiac myocytes is
unknown. However, localization of connexin-43 likely involves an
interaction with the cytoskeleton; immunofluorescence microscopy showed
that in cardiac myocytes, connexin-43 specifically colocalizes with the
cytoskeletal proteins ZO-1 and 
-spectrin. In transfected HEK293
cells, immunoprecipitation experiments using coexpressed epitope-tagged
connexin-43 and ZO-1 indicated that ZO-1 links connexin-43 with
-spectrin. The domains responsible for the protein-protein interaction between connexin-43 and ZO-1 were identified using affinity
binding assays with deleted ZO-1 and connexin-43 fusion proteins.
Immunoblot analysis of associated proteins showed that the C-terminal
domain of connexin-43 binds to the N-terminal domain of ZO-1. The role
of this linkage in gap junction formation was examined by a
dominant-negative assay using the N-terminal domain of ZO-1.
Overexpression of the N-terminal domain of ZO-1 in
connexin-43-expressing cells resulted in redistribution of connexin-43
from cell-cell interfaces to cytoplasmic structures; this intracellular
redistribution of connexin-43 coincided with a loss of electrical
coupling. We therefore conclude that the linkage between connexin-43
and -spectrin, via ZO-1, may serve to localize connexin-43 at the
intercalated discs, thereby generating functional gap junctions in
cardiac myocytes.
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