MAPK/ERK-dependent Munc18-1 phosphorylation in the neuromuscular junction

Identifier:  TFG:6031

Handle: https://hdl.handle.net/20.500.11797/TFG6031

Authors:  Rayo Morales, Mario Andrés

Abstract:
Munc18 -1, which is phosphorylated in Ser241 by extracellular-regulated kinase (ERK), is a presynaptic protein involved in the regulation of the acetylcholine release in the neuromuscular junction (NMJ). The objective of this work is to determine whether the neuromuscular activity regulates the ERK pathway in the nerve terminal, and the role of M2 muscarinic acetylcholine receptor in this regulation. Using presynaptic stimulated rat diaphragms, results showed that (1) presynaptic activity decreases ERK-dependent Munc18-1 phosphorylation whereas nerve-induced contraction promotes it; and (2) this ERK activity is modulated through M2. In summary, ERK-dependent Munc18-1 phosphorylation is differently regulated during neuromuscular activity through M2.