PDZ domains and the organization of supramolecular complexes

Authors
Citation
M. Sheng et C. Sala, PDZ domains and the organization of supramolecular complexes, ANN R NEUR, 24, 2001, pp. 1-29
Citations number
143
Categorie Soggetti
Neurosciences & Behavoir
Journal title
ANNUAL REVIEW OF NEUROSCIENCE
ISSN journal
0147006X → ACNP
Volume
24
Year of publication
2001
Pages
1 - 29
Database
ISI
SICI code
0147-006X(2001)24:<1:PDATOO>2.0.ZU;2-V
Abstract
PDZ domains are modular protein interaction domains that bind in a sequence -specific fashion to short C-terminal peptides or internal peptides that fo ld in a beta -finger. The diversity of PDZ binding specificities can be exp lained by variable amino acids lining the peptide-binding groove of the PDZ domain. Abundantly represented in Caenorhabditis elegans, Drosophila melan ogaster, and mammalian genomes, PDZ domains are frequently found in multipl e copies or are associated with other protein-binding motifs in multidomain scaffold proteins. PDZ-containing proteins are typically involved in the a ssembly of supramolecular complexes that perform localized signaling functi ons at particular subcellular locations. Organization around a PDZ-based sc affold allows the stable localization of interacting proteins and enhances the rate and fidelity of signal transduction within the complex. Some PDZ-c ontaining proteins are more dynamically regulated in distribution and may a lso be involved in the trafficking of interacting proteins within the cell.