ERK activation by G-protein-coupled receptors in mouse brain is receptor identity-specific.

Vanhoose AM, Emery M, Jimenez L, Winder DG
J Biol Chem. 2002 277 (11): 9049-53

PMID: 11782465 · DOI:10.1074/jbc.M108309200

In transfected cells and non-neuronal tissues many G-protein-coupled receptors activate p44/42 MAP kinase (ERK), a kinase involved in both hippocampal synaptic plasticity and learning and memory. However, it is not clear to what degree these receptors couple to ERK in brain. G(s)-coupled beta-adrenergic receptor activation of ERK in neurons is critical in the regulation of synaptic plasticity in area CA1 of the hippocampus. In addition, alpha(1)- and alpha(2)-adrenergic receptors, present in CA1, could potentially activate ERK. We find that, like the beta-adrenergic receptor, the G(q)-coupled alpha(1)AR activates ERK in adult mouse CA1. However, activation of the G(i/o)-coupled alpha(2)AR does not activate ERK, nor does activation of a homologous G(i/o)-coupled receptor enriched in adult mouse CA1, the 5HT(1A) receptor. In contrast, the nonhomologous G(i/o)-coupled gamma-aminobutyric acid type B receptor does activate ERK in adult mouse CA1. Surprisingly, activation of alpha(2)ARs in CA1 from immature animals where basal phospho-ERK is low induces ERK phosphorylation. These data suggest that although most G-protein-coupled receptor subtypes activate ERK in non-neuronal cells, the coupling of G(i/o) to ERK is tightly regulated in brain.

MeSH Terms (12)

Animals Brain Enzyme Activation GTP-Binding Proteins Mice Mice, Inbred C57BL Mitogen-Activated Protein Kinases Phosphorylation Receptors, Adrenergic, alpha-2 Receptors, Adrenergic, beta-1 Receptors, Cell Surface Receptors, GABA-B

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