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

Marius Sudol, Claudia C. Recinos, Jennifer Abraczinskas, Jasper Humbert, Amjad Farooq

Research output: Contribution to journalReview articlepeer-review

43 Scopus citations


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.

Original languageEnglish
Pages (from-to)773-778
Number of pages6
JournalIUBMB Life
Issue number12
StatePublished - Dec 2005


  • High-resolution structures of domains
  • Inter-domain linkers
  • Modular domains
  • Proteomic arrays
  • Tandem domains


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