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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Calcium Channels / metabolism
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Drosophila
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Drosophila Proteins*
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Electrophysiology
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Eye Proteins / chemistry
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Eye Proteins / genetics
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Eye Proteins / metabolism*
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Female
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GTP-Binding Proteins / metabolism*
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Insect Proteins / metabolism
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Male
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Molecular Sequence Data
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Mutation
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Photoreceptor Cells, Invertebrate / metabolism
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Photoreceptor Cells, Invertebrate / ultrastructure
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Protein Kinase C / metabolism
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Sequence Homology, Amino Acid
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Signal Transduction*
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Transient Receptor Potential Channels
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Type C Phospholipases / metabolism
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Vision, Ocular
Substances
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Calcium Channels
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Drosophila Proteins
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Eye Proteins
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Insect Proteins
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Transient Receptor Potential Channels
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inaD protein, Drosophila
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trp protein, Drosophila
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Protein Kinase C
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Type C Phospholipases
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GTP-Binding Proteins