RT Journal Article
SR Electronic
T1 Requirement for Tyrosine Phosphatase during Serotonergic Neuromodulation by Protein Kinase C
JF The Journal of Neuroscience
JO J. Neurosci.
FD Society for Neuroscience
SP 5792
OP 5797
DO 10.1523/JNEUROSCI.17-15-05792.1997
VO 17
IS 15
A1 Stefano Catarsi
A1 Pierre Drapeau
YR 1997
UL http://www.jneurosci.org/content/17/15/5792.abstract
AB Tyrosine kinases and phosphatases are abundant in the nervous system, where they signal cellular differentiation, mediate the responses to growth factors, and direct neurite outgrowth during development. Tyrosine phosphorylation can also alter ion channel activity, but its physiological significance remains unclear. In an identified leech mechanosensory neuron, the ubiquitous neuromodulator serotonin increases the activity of a cation channel by activating protein kinase C (PKC), resulting in membrane depolarization and modulation of the receptive field properties. We observed that the effects on isolated neurons and channels were blocked by inhibiting tyrosine phosphatases. Serotonergic stimulation of PKC thus activates a tyrosine phosphatase activity associated with the channels, which reverses their constitutive inhibition by tyrosine phosphorylation, representing a novel form of neuromodulation.