Abstract
WW domains are small protein modules that recognize proline-rich peptide motifs or phosphorylated-serine/threonine proline sites in cognate proteins. Within host proteins these modules are joined to other protein domains or to a variety of catalytic domains acting together as adaptors or targeting anchors of enzymes. An important aspect of signaling by WW domains is their ability to recognize their cognate ligands in tandem. Tandem WW domains not only act in a synergistic manner but also appear to chaperone the function of each other. In this review, we focus on structure, function, and mechanism of the tandem WW domains co-operativity as well as independent actions. We emphasize here the implications of tandem arrangement and cooperative function of the domains for signaling pathways.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adaptor Proteins, Signal Transducing / metabolism
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ErbB Receptors / metabolism
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Models, Molecular*
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Oxidoreductases / metabolism
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Phosphoproteins / metabolism
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Proline / metabolism
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Protein Binding
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Protein Structure, Tertiary / genetics*
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Proteins / chemistry*
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Receptor, ErbB-4
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Signal Transduction / genetics*
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Transcription Factors
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Tryptophan / chemistry
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Tumor Suppressor Proteins
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WW Domain-Containing Oxidoreductase
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YAP-Signaling Proteins
Substances
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Adaptor Proteins, Signal Transducing
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Phosphoproteins
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Proteins
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Transcription Factors
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Tumor Suppressor Proteins
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YAP-Signaling Proteins
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YAP1 protein, human
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Tryptophan
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Proline
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Oxidoreductases
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WW Domain-Containing Oxidoreductase
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WWOX protein, human
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ERBB4 protein, human
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ErbB Receptors
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Receptor, ErbB-4