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J. Cell Biol.,
Volume 142, Number 2, July 27, 1998 545-555
Department of Biological Chemistry and Department of Neuroscience, The Johns Hopkins University School of Medicine,
Baltimore, Maryland 21205
The rapid activation and feedback regulation
of many G protein signaling cascades raises the possibility that the critical signaling proteins may be tightly
coupled. Previous studies show that the PDZ domain
containing protein INAD, which functions in Drosophila vision, coordinates a signaling complex by binding directly to the light-sensitive ion channel, TRP, and to
phospholipase C (PLC). The INAD signaling complex
also includes rhodopsin, protein kinase C (PKC), and
calmodulin, though it is not known whether these proteins bind to INAD. In the current work, we show that rhodopsin, calmodulin, and PKC associate with the signaling complex by direct binding to INAD. We also
found that a second ion channel, TRPL, bound to
INAD. Thus, most of the proteins involved directly in
phototransduction appear to bind to INAD. Furthermore, we found that INAD formed homopolymers and
the homomultimerization occurred through two PDZ
domains. Thus, we propose that the INAD supramolecular complex is a higher order signaling web consisting
of an extended network of INAD molecules through
which a G protein-coupled cascade is tethered.
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