Protein tyrosine kinase PYK2 involved in Ca2+-induced regulation of ion channel and MAP kinase functions

  title={Protein tyrosine kinase PYK2 involved in Ca2+-induced regulation of ion channel and MAP kinase functions},
  author={Sima Lev and Herman Moreno and Rhysly Martinez and P D Canoll and Elior Peles and Jos{\'e} M. Musacchio and Gregory D. Plowman and Bernardo Rudy and Joseph Schlessinger},
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… 

Novel form of crosstalk between G protein and tyrosine kinase pathways.

It is shown that the inhibition of sensory neuron N-type Ca2+ channels produced by gamma-aminobutyric acid involves a novel, rapidly activating tyrosine kinase signaling pathway that is mediated by Galphao and a src-like kinase.

Regulation of ion channels by protein tyrosine phosphorylation.

This review presents a comprehensive summary and synthesis of the literature regarding the mechanism and function of ion channel regulation by protein tyrosine kinases and phosphatases, and discusses the critical roles that channel-associated scaffolding proteins may play in localizing protein tyrolysis and phosphorylation to the vicinity of ion channels.

Expression of Voltage-Gated Potassium Channels Decreases Cellular Protein Tyrosine Phosphorylation

The results suggest that reciprocal modulatory interactions occur between Kv channel and protein tyrosine phosphorylation signaling pathways.

Regulation of potassium channels by protein kinases

Protein tyrosine kinase-mediated pathways in G protein-coupled receptor signaling

Novel insights in chemokine receptor-activated PTKs and their role in mediating cell functions are discussed in this review.

Tyrosine kinases in activation of the MAP kinase cascade by G-protein-coupled receptors

It is shown that in cells deficient in the Src-related tyrosine kinase Lyn, stimulation of MAPK kinase and MAPK by Gq-coupled ml muscarinic acetylcholine receptors (mAChR) is blocked, whereas Gicoupled m2 mAChR-mediated stimulation is unaffected.

Cyclic AMP and Tyrosine Kinase Cascades in the Regulation of Cellular Function by P2Y Nucleotide Receptors

The emerging, and apparently widespread, role of tyrosine phosphorylation cascades in the control of cellular function by the G protein-coupled P2Y receptors is considered, focusing on the role of mitogen activated protein kinases (MAPK).

Activation of protein tyrosine kinase PYK2 by the m1 muscarinic acetylcholine receptor.

PYK2 is established as an effector of the m1 muscarinic receptor in the regulation of multiple cell functions and specifically phosphorylates the carboxyl-terminal cytosolic portion of the potassium channel Kv1.2 in a manner regulated by them1 receptor.



Regulation of NMDA receptors by tyrosine kinases and phosphatases

Evidence is presented that in mammalian central neurons tyrosine phosphorylation regulates the function of the NMDA (N-methyl-D-aspartate) receptor, a subtype of excitatory amino-acid receptor, which may be important in neuronal development, plasticity and toxicity.

Convergent regulation of sodium channels by protein kinase C and cAMP-dependent protein kinase.

The function of voltage-gated sodium channels that are responsible for action potential generation in mammalian brain neurons is modulated by phosphorylation by adenosine 3',5'-monophosphate

Calcium-dependent increase in tyrosine kinase activity stimulated by angiotensin II.

  • W. HuckleR. DyH. Earp
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1992
A link between two widely occurring signaling pathways, the tyrosine kinases and the Ca2+ second-messenger system, is demonstrated and the possible involvement of Ca(2+)-activated tyrosin kinases in the endocrine actions of AngII and [Arg8]vasopressin is suggested.

Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling

The results indicate that the Grbl/hSos1 complex couples activated EGF receptor to Ras signalling, and a synthetic 10-amino-acid peptide containing the sequence PPVPPR specifically blocks the interaction.