A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade - PubMed (original) (raw)

. 1997 Jul 17;388(6639):243-9.

doi: 10.1038/40805.

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

S Tsunoda et al. Nature. 1997.

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-beta 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 'transduclisome', with PDZ domains functioning as key elements in the organization of transduction complexes in vivo.

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