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WW or WoW: The WW domains in a union of bliss
Author(s) -
Sudol Marius,
Recinos Claudia C.,
Abraczinskas Jennifer,
Humbert Jasper,
Farooq Amjad
Publication year - 2005
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540500389039
Subject(s) - ww domain , tandem repeat , phosphorylation , function (biology) , serine , threonine , microbiology and biotechnology , chemistry , biology , biochemistry , genome , gene
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.