PDZ domain proteins: scaffolds for signaling complexes.

Current biology : CB ·Vol. 7 ·No. 12 ·1997-12-01 ·Pages R770-3

Ranganathan R, Ross EM

Abstract

InaD, a Drosophila photoreceptor scaffolding protein, assembles multiple signal-transducing proteins at the membrane via its five PDZ domains, enhancing speed and efficiency of vision. Extensive conservation of PDZ domains suggests that these motifs have a general role in organizing diverse signaling complexes.

MeSH Terms

Animals Binding Sites Calcium Channels/metabolism Drosophila Drosophila Proteins Eye Proteins/metabolism GTP-Binding Proteins/metabolism Photoreceptor Cells, Invertebrate/metabolism Protein Kinase C/metabolism Signal Transduction TRPC Cation Channels Type C Phospholipases/metabolism

Chemicals

Calcium Channels Drosophila Proteins Eye Proteins TRPC Cation Channels inaD protein, Drosophila transient receptor potential cation channel, subfamily C, member 1 Protein Kinase C Type C Phospholipases GTP-Binding Proteins

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Ranganathan R

Howard Hughes Medical Institute, Department of Pharmacology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75235-9041, USA. [email protected]

Ross E M

Article Info

Journal

Current biology : CB

Abbr.

Curr Biol

ISSN

0960-9822

DOI

10.1016/s0960-9822(06)00401-5

[email protected]

Published

1997-12-01

Pages

R770-3

Language

English

Region

England

NLM ID

9107782

Subset

External Links

PubMed source DOI: 10.1016/s0960-9822(06)00401-5 View journal details

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PDZ domain proteins: scaffolds for signaling complexes.

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