title: Calcium-dependent Pyk2 activation: a role for calmodulin?
abstract: Pyk2 (proline-rich tyrosine kinase 2) and FAK (focal adhesion kinase) are highly related tyrosine kinases. One distinguishing feature is the differential regulation of the two enzymes in response to elevation of cytoplasmic calcium. In the latest issue of the Biochemical Journal, Sasaki and co-workers have provided insight into the calcium-dependent regulation of Pyk2. The findings suggest that calmodulin may bind the FERM (4.1/ezrin/radixin/moesin) domain to promote Pyk2 activation in response to calcium signals triggered by vasopressin. While the molecular details of the protein-protein interaction and mechanism of activation remain to be firmly established, this study is the first to provide mechanistic insight into the regulation of Pyk2 by calcium.
authors.affiliation: Lineberger Comprehensive Cancer Center, Carolina Cardiovascular Biology Center, Comprehensive Center for Inflammatory Disorders, 534 Taylor Hall, CB 7090, University of North Carolina, Chapel Hill, NC 5799, USA. email crispy4@med.unc.edu
authors.forename: Michael D
authors.initials: MD
authors.lastname: Schaller
mesh_terms: D002118:Calcium / Q000378:metabolism*; D002147:Calmodulin / Q000502:physiology*; D004789:Enzyme Activation; D051418:Focal Adhesion Kinase 2 / Q000737:chemistry / Q000378:metabolism*
chemical_list: D002147:Calmodulin; D051418:Focal Adhesion Kinase 2; D002118:Calcium