FMRFamide reverses protein phosphorylation produced by 5-HT and cAMP in Aplysia sensory neurons

Détails

ID Serval
serval:BIB_FDF5ACAB7C4C
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
FMRFamide reverses protein phosphorylation produced by 5-HT and cAMP in Aplysia sensory neurons
Périodique
Nature
Auteur(s)
Sweatt  J. D., Volterra  A., Edmonds  B., Karl  K. A., Siegelbaum  S. A., Kandel  E. R.
ISSN
0028-0836 (Print)
Statut éditorial
Publié
Date de publication
11/1989
Volume
342
Numéro
6247
Pages
275-8
Notes
In Vitro
Journal Article --- Old month value: Nov 16
Résumé
Neurotransmitter can modulate neuronal activity through a variety of second messengers that act on ion channels and other substrate proteins. The most commonly described effector mechanism for second messengers in neurons depends on protein phosphorylation mediated by one of three sets of kinases: the cyclic AMP-dependent protein kinases, the Ca2+-calmodulin-dependent protein kinases, and the Ca2+-phospholipid-dependent protein kinases. In addition, some neurotransmitters and second messengers can also inhibit protein phosphorylation by lowering cAMP levels (either by inhibiting adenylyl cyclase or activating phosphodiesterases). This raises the question: can neurotransmitters also modulate neuronal activity by decreasing protein phosphorylation that is independent of cAMP? Various biochemical experiments show that a decrease in protein phosphorylation can arise through activation of a phosphatase or inhibition of kinases. In none of these cases, however, is the physiological role for the decrease in protein phosphorylation known. Here we report that in Aplysia sensory neurons, the presynaptic inhibitory transmitter FMRFamide decreases the resting levels of protein phosphorylation without altering the level of cAMP. Furthermore, FMRFamide overrides the cAMP-mediated enhancement of transmitter release produced by 5-hydroxytryptamine (5-HT), and concomitantly reverses the cAMP-dependent increase in protein phosphorylation produced by 5-HT. These findings indicate that a receptor-mediated decrease in protein phosphorylation may play an important part in the modulation of neurotransmitter release.
Mots-clé
Animals Aplysia Cyclic AMP/*pharmacology Electric Conductivity Electrophoresis, Gel, Two-Dimensional FMRFamide Isoelectric Point Molecular Weight Nerve Tissue Proteins/*metabolism Neural Inhibition Neuropeptides/*pharmacology Phosphoproteins/*metabolism Potassium Channels/physiology Serotonin/*pharmacology
Pubmed
Web of science
Création de la notice
24/01/2008 15:37
Dernière modification de la notice
20/08/2019 17:28
Données d'usage