A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade

Susan Tsunoda, Jimena Sierralta, Yumei Sun, Ruth Bodner, Emiko Suzuki, Ann Becker, Michael Socolich and Charles S. Zuker ()
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Susan Tsunoda: University of California at San Diego
Jimena Sierralta: University of California at San Diego
Yumei Sun: University of California at San Diego
Ruth Bodner: University of California at San Diego
Emiko Suzuki: *The Insitute of Medical Science, The University of Tokyo
Ann Becker: University of California at San Diego
Michael Socolich: University of California at San Diego
Charles S. Zuker: University of California at San Diego

Nature, 1997, vol. 388, issue 6639, 243-249

Abstract: Abstract How are signalling molecules organized into different pathways within the same cell? In Drosophila, the inaD gene encodes a protein consisting of five PDZ domains which serves as a scaffold to assemble different components of the phototransduction cascade, including the principal light-activated ion channels, the effector phospholipase C-β and protein kinase C. Null inaD mutants have a dramatically reorganized subcellular distribution of signalling molecules, and a total loss of transduction complexes. Also, mutants defective in a single PDZ domain produce signalling complexes that lack the target protein and display corresponding defects in their physiology. A picture emerges of a highly organized unit of signalling, a ‘transducisome’, with PDZ domains functioning as key elements in the organization of transduction complexes in vivo.

Date: 1997
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DOI: 10.1038/40805

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