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Mechanism and role of PDZ domains in signaling complex assembly

Journal of Cell Science · 2001 · Vol. 114(18) · pp. 3219–3231
Baruch Z. HarrisWendell A. Lim

Abstract

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.

Hippo pathway signaling and YAP/TAZNeurobiology and Insect Physiology ResearchUbiquitin and proteasome pathwaysPDZ domainBiologyMulticellular organismScaffold proteinCell biologySignal transductionMechanism (biology)CellBiochemistry

MeSH terms

AnimalsBinding SitesDrosophila melanogasterHumansLigandsMembrane ProteinsModels, ChemicalNerve Tissue ProteinsPhosphoproteinsSignal TransductionCaenorhabditis elegansSequence HomologyProtein Structure, TertiaryInsect ProteinsAmino Acid Motifs
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References
The Sequence of the Human Genome
Science · 2001 · 13,619 citations
The Protein Data Bank
Nucleic Acids Research · 2000 · 39,191 citations
Initial sequencing and analysis of the human genome
Nature · 2001 · 24,452 citations
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