• Register
X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X

Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.

No
Yes

Identification and localization of a skeletal muscle secrotonin 5-HT2A receptor coupled to the Jak/STAT pathway.

The neurotransmitter serotonin mediates a wide variety of peripheral and central physiological effects through the binding to multiple receptor subtypes (Wilkinson, L. O., and Dourish, C. T. (1991) in Serotonin Receptor Subtypes: Basic and Clinical Aspects (Peroutka, S. J., ed) Vol. 15, pp.147-210, Wiley-Liss, New York). Among them, serotonin 5-HT2A receptors are known to activate the phospholipase C-beta second messenger pathway (Peroutka, S. J. (1995) Trends Neurosci. 18, 68-69). We identified and localized in rat skeletal muscle myoblasts a functional serotonin 5-HT2A receptor. This receptor was detected on the plasma membrane, in myoblasts, and at the level of T-tubules in contracting myotubes. Binding of serotonin to its receptor increases the expression of genes involved in myogenic differentiation. Unexpectedly, the 5-HT2A receptor is able to activate another signaling pathway; it triggers a rapid and transient tyrosine phosphorylation of Jak2 kinase in response to serotonin. Jak2 auto-phosphorylation is followed by the tyrosine phosphorylation of STAT3 (signal transducers and activators of transcription) and its translocation into the nucleus. We also find that the 5-HT2A receptor and STAT3 co-precipitate with Jak2, indicating that they are physically associated. We conclude that the serotonin 5-HT2A receptor identified in skeletal muscle myoblasts is able to activate the intracellular phosphorylation pathway used by cytokines. The presence of serotonin receptors in T-tubules suggests a role for serotonin in excitation-contraction coupling and (or) an effect in skeletal muscle fiber repairing.

Pubmed ID: 9169451

Authors

  • Guillet-Deniau I
  • Burnol AF
  • Girard J

Journal

The Journal of biological chemistry

Publication Data

June 6, 1997

Associated Grants

None

Mesh Terms

  • Animals
  • Base Sequence
  • Cell Membrane
  • Cells, Cultured
  • DNA-Binding Proteins
  • Fetus
  • Glucose Transporter Type 1
  • Glucose Transporter Type 2
  • Janus Kinase 2
  • Molecular Sequence Data
  • Monosaccharide Transport Proteins
  • Muscle, Skeletal
  • Myogenin
  • Phosphorylation
  • Polymerase Chain Reaction
  • Protein-Tyrosine Kinases
  • Proto-Oncogene Proteins
  • Rats
  • Receptor, Serotonin, 5-HT2A
  • Receptors, Serotonin
  • STAT3 Transcription Factor
  • Serotonin
  • Signal Transduction
  • Trans-Activators
  • Transcription, Genetic