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

• 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
• ISSN: 1521-6543; 1521-6551
• DOI: 10.1080/15216540500389039

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.