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J Biol Chem, Vol. 273, Issue 52, 34671-34674, December 25, 1998
Signaling
From the Department of Cell Biology and Vanderbilt Cancer Center,
Vanderbilt University School of Medicine,
Nashville, Tennessee 37232-6838
Transforming growth factor-
1 (TGF-1) is the
prototype of a large family of proteins that regulate a variety of
biological processes. The pleiotropic responses to TGF- are mediated
via ligand-induced heteromeric complex formation by type I (TR-I) and type II (TR-II) serine-threonine kinase receptors. Several studies have shown that TR-II acts as a primary receptor, binding TGF- and phosphorylating TR-I, whose kinase activity then
propagates the signals. Therefore, intracellular proteins that interact
with type I receptors are likely to play important roles in TGF-
signaling. We have identified a novel WD domain-containing protein,
designated STRAP (serine-threonine kinase
receptor-associated protein), which interacts with TR-I in a yeast two-hybrid system. STRAP associates with both functional TR-I and TR-II in vivo.
Overexpression of STRAP leads to inhibition of TGF--mediated
transcriptional activation. It also shows synergistic inhibition of
TGF- signaling in concert with Smad7, but not with Smad6, as
measured by TGF--dependent transcriptional reporters.
The existence of the STRAP gene from yeast to mammals indicates an
evolutionarily conserved function in eukaryotes. The data suggest a
potential role for STRAP in TGF- signal transduction.
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