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Vol. 273, Issue 2, 677-680, January 9, 1998
From the Department of Biological Chemistry, University of
Michigan, Ann Arbor, Michigan 48109-0606
The Smad family of intracellular proteins
mediates signals generated by activin and other transforming growth
factor 
-related proteins via specific heteromeric complexes of
transmembrane receptor serine kinases (1, 2). xSmad2 has been
implicated as an activin signal mediator that may participate in
transcriptional regulation (3, 4). We have employed an interaction
cloning strategy to identify xSmad2-binding proteins and found that
calmodulin directly associated with Smads. xSmad2, generated either by
in vitro translation or by overexpression in COS cells,
specifically bound to calmodulin-agarose; the association was
calcium-dependent and required xSmad2 N-terminal residues.
In the same assay, xSmad1 and hSmads 2, 3, and 4 also bound to
calmodulin-agarose. Furthermore, a calmodulin antagonist, W13,
increased expression of the activin-inducible transcriptional reporter,
3TP-Lux, whereas overexpression of calmodulin suppressed this reporter.
These observations demonstrate that Smad proteins interact with
calmodulin in a calcium-dependent way through conserved N-terminal amino acids and suggest a role for calmodulin in regulating Smad function.
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