Protein tyrosine kinase PYK2 involved in Ca2+-induced regulation of ion channel and MAP kinase functions
- 1 August 1995
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 376 (6543) , 737-745
Abstract
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.Keywords
This publication has 44 references indexed in Scilit:
- Elimination of rapid potassium channel inactivation by phosphorylation of the inactivation gateNeuron, 1994
- Receptor Protein-Tyrosine Kinases and Their Signal Transduction PathwaysAnnual Review of Cell Biology, 1994
- Tyrosine kinase-dependent suppression of a potassium channel by the G protein-coupled m1 muscarinic acetylcholine receptorCell, 1993
- Convergent regulation of sodium channels by protein kinase C and cAMP-dependent protein kinaseScience, 1993
- A non-receptor tyrosine kinase that inhibits the GTPase activity of p21cdc42Nature, 1993
- Growth factor signaling by receptor tyrosine kinasesNeuron, 1992
- Long-term potentiation in the hippocampus is blocked by tyrosine kinase inhibitorsNature, 1991
- Protein tyrosine kinases and phosphatases in the nervous systemCurrent Opinion in Neurobiology, 1991
- The trk proto-oncogene encodes a receptor for nerve growth factorCell, 1991
- Activation of chloride channels in normal and cystic fibrosis airway epithelial cells by multifunctional calcium/calmodulin-dependent protein kinaseNature, 1991