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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 18
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pubmed:dateCreated |
2001-10-9
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/discs large 1 protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/postsynaptic density proteins,
http://linkedlifedata.com/resource/pubmed/chemical/zonula occludens-1 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9533
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
114
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3219-31
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading |
pubmed-meshheading:11591811-Amino Acid Motifs,
pubmed-meshheading:11591811-Animals,
pubmed-meshheading:11591811-Binding Sites,
pubmed-meshheading:11591811-Caenorhabditis elegans,
pubmed-meshheading:11591811-Drosophila Proteins,
pubmed-meshheading:11591811-Drosophila melanogaster,
pubmed-meshheading:11591811-Humans,
pubmed-meshheading:11591811-Insect Proteins,
pubmed-meshheading:11591811-Ligands,
pubmed-meshheading:11591811-Macromolecular Substances,
pubmed-meshheading:11591811-Membrane Proteins,
pubmed-meshheading:11591811-Models, Chemical,
pubmed-meshheading:11591811-Nerve Tissue Proteins,
pubmed-meshheading:11591811-Phosphoproteins,
pubmed-meshheading:11591811-Protein Structure, Tertiary,
pubmed-meshheading:11591811-Sequence Homology,
pubmed-meshheading:11591811-Signal Transduction,
pubmed-meshheading:11591811-Tumor Suppressor Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
Mechanism and role of PDZ domains in signaling complex assembly.
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pubmed:affiliation |
Department of Cellular and Molecular Pharmacology, University of California San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143-0450, USA.
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pubmed:publicationType |
Journal Article,
Review
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