PDZ domain proteins: scaffolds for signaling complexes (Q28255429)

Signal Transduction in Drosophila Photoreceptors

Europe PubMed Central

title

PDZ domain proteins: scaffolds for signaling complexes (English)

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author name string

R Ranganathan

series ordinal

1

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E M Ross

series ordinal

2

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language of work or name

English

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publication date

1 December 1997

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published in

Current Biology

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volume

7

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issue

12

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page(s)

R770-3

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cites work

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Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex

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

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A Drosophila mutant defective in extracellular calcium-dependent photoreceptor deactivation and rapid desensitization.

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The trp gene is essential for a light-activated Ca2+ channel in Drosophila photoreceptors.

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Photoreceptor deactivation and retinal degeneration mediated by a photoreceptor-specific protein kinase C.

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A novel protein encoded by the InaD gene regulates recovery of visual transduction in Drosophila

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The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein

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Clustering membrane proteins: It's all coming together with the PSD-95/SAP90 protein family

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Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases

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Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95

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Recognition of unique carboxyl-terminal motifs by distinct PDZ domains

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Crystal structure of a PDZ domain

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Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ

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GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors

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PDZ domains: targeting signalling molecules to sub-membranous sites

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Molecular characterization of a novel human PDZ domain protein with homology to INAD from Drosophila melanogaster

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