Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions

• Published in: Nature (London) Vol. 376; no. 6543; pp. 737 - 745
• Main Authors: Lev, S, Moreno, H, Martinez, R, Canoll, P, Peles, E, Musacchio, J M, Plowman, G D, Rudy, B, Schlessinger, J
• Format: Journal Article
• Language: English
• Published: England 31.08.1995
• Subjects: 3T3 Cells; Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Animals; Base Sequence; Brain - enzymology; Calcium - metabolism; Cells, Cultured; Cloning, Molecular; DNA Primers; Enzyme Activation; Focal Adhesion Kinase 2; GRB2 Adaptor Protein; GTP-Binding Proteins - metabolism; Humans; Ion Channels - metabolism; Kv1.2 Potassium Channel; Mice; Molecular Sequence Data; PC12 Cells; Phosphorylation; Potassium Channels - metabolism; Potassium Channels, Voltage-Gated; Protein Kinase C - metabolism; Protein Kinases - metabolism; Protein-Tyrosine Kinases - drug effects; Protein-Tyrosine Kinases - metabolism; Proteins - metabolism; Rats; Tyrosine - metabolism
• ISSN: 0028-0836
• DOI: 10.1038/376737a0

The protein tyrosine kinase PYK2, which is highly expressed in the central nervous system, is rapidly phosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration, as well as by protein kinase C activation. Activation of PYK2 leads to modulation of ion channel function and activation of the MAP kinase signalling pathway. PYK2 activation may provide a mechanism for a variety of short- and long-term calcium-dependent signalling events in the nervous system.