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Journal of Cell Science 114, 3219-3231 (2001)
© 2001 The Company of Biologists Limited


COMMENTARY

Mechanism and role of PDZ domains in signaling complex assembly

Baruch Z. Harris and Wendell A. Lim*

Department of Cellular and Molecular Pharmacology, University of California San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143-0450, USA

*Author for correspondence (e-mail: wlim{at}itsa.ucsf.edu)

PDZ domains are protein-protein recognition modules that play a central role in organizing diverse cell signaling assemblies. These domains specifically recognize short C-terminal peptide motifs, but can also recognize internal sequences that structurally mimic a terminus. PDZ domains can therefore be used in combination to bind an array of target proteins or to oligomerize into branched networks. Several PDZ-domain-containing proteins play an important role in the transport, localization and assembly of supramolecular signaling complexes. Examples of such PDZ-mediated assemblies exist in Drosophila photoreceptor cells and at mammalian synapses. The predominance of PDZ domains in metazoans indicates that this highly specialized scaffolding module probably evolved in response to the increased signaling needs of multicellular organisms.

Key words: PDZ, Signaling, Scaffolding




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