WW or WoW: The WW domains in a union of bliss

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 a...

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Bibliographic Details
Published in:IUBMB life 2005-12, Vol.57 (12), p.773-778
Main Authors: Sudol, Marius, Recinos, Claudia C., Abraczinskas, Jennifer, Humbert, Jasper, Farooq, Amjad
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing - metabolism
ErbB Receptors - metabolism
high‐resolution structures of domains
inter‐domain linkers
Models, Molecular
Modular domains
Oxidoreductases - metabolism
Phosphoproteins - metabolism
Proline - metabolism
Protein Binding
Protein Structure, Tertiary - genetics
Proteins - chemistry
proteomic arrays
Receptor, ErbB-4
Signal Transduction - genetics
tandem domains
Transcription Factors
Tryptophan - chemistry
Tumor Suppressor Proteins
WW Domain-Containing Oxidoreductase
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Summary: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.
ISSN:1521-6543
1521-6551
DOI:10.1080/15216540500389039