QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

This Article Full Text Full Text (PDF) Submit an eLetter Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Web of Science (15) Citing Articles via Google Scholar Google Scholar Articles by Catarsi, S. Articles by Drapeau, P. Search for Related Content PubMed PubMed Citation Articles by Catarsi, S. Articles by Drapeau, P.

 Previous Article  |  Next Article 

Volume 17, Number 15, Issue of August 1, 1997 pp. 5792-5797
Copyright ©1997 Society for Neuroscience

Requirement for Tyrosine Phosphatase during Serotonergic Neuromodulation by Protein Kinase C

Received March 7, 1997; revised May 6, 1997; accepted May 20, 1997.

Stefano Catarsi and Pierre Drapeau

Centre for Research in Neuroscience, McGill University, and Montreal General Hospital Research Institute, Montreal, Quebec, Canada H3G 1A4

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.

Key words: single channel; serotonin; protein kinase C; tyrosine phosphorylation; identified neuron; leech

This article has been cited by other articles:

				H. Sheng, Y. Zhang, J. Sun, L. Gao, B. Ma, J. Lu, and X. Ni Corticotropin-Releasing Hormone (CRH) Depresses N-Methyl-D-Aspartate Receptor-Mediated Current in Cultured Rat Hippocampal Neurons via CRH Receptor Type 1 Endocrinology, March 1, 2008; 149(3): 1389 - 1398. [Abstract] [Full Text] [PDF]

				S.-J. Pan, M. Zhu, M. K. Raizada, C. Sumners, and C. H. Gelband ANG II-mediated inhibition of neuronal delayed rectifier K+ current: role of protein kinase C-{alpha} Am J Physiol Cell Physiol, July 1, 2001; 281(1): C17 - C23. [Abstract] [Full Text] [PDF]

				B. D. Burrell, C. L. Sahley, and K. J. Muller Non-Associative Learning and Serotonin Induce Similar Bi-Directional Changes in Excitability of a Neuron Critical for Learning in the Medicinal Leech J. Neurosci., February 15, 2001; 21(4): 1401 - 1412. [Abstract] [Full Text] [PDF]

				J Harvey and M L J Ashford Role of tyrosine phosphorylation in leptin activation of ATP-sensitive K+ channels in the rat insulinoma cell line CRI-G1 J. Physiol., July 1, 1998; 510(1): 47 - 61. [Abstract] [Full Text] [PDF]

				D. W Ali, S. Catarsi, and P. Drapeau Ionotropic and metabotropic activation of a neuronal chloride channel by serotonin and dopamine in the leech Hirudo medicinalis J. Physiol., May 15, 1998; 509(1): 211 - 219. [Abstract] [Full Text] [PDF]

				M. Levy, J. Jing, D. Chikvashvili, W. B. Thornhill, and I. Lotan Activation of a Metabotropic Glutamate Receptor and Protein Kinase C Reduce the Extent of Inactivation of the K+ Channel Kv1.1/Kvbeta 1.1 via Dephosphorylation of Kv1.1 J. Biol. Chem., March 13, 1998; 273(11): 6495 - 6502. [Abstract] [Full Text] [PDF]

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help