Dual signaling is differentially activated by different active states of the metabotropic glutamate receptor 1alpha.

ABSTRACT: The metabotropic glutamate receptor 1alpha (mGluR1alpha) is crucial for some forms of synaptic plasticity, by inducing various cell responses via coupling to various types of G proteins. Upon glutamate binding, an active conformation, closed-open/active, of the extracellular domain is stabilized, which induces dimeric rearrangement in the intracellular domains, resulting in the initiation of downstream signals. We have confirmed that mGluR1alpha functionally interacts with both Gq and Gs pathways; a combination of fluorescent indicators showed that glutamate increased intracellular Ca(2+) and cAMP concentration ([Ca(2+)](i) and [cAMP](i)). By contrast, Gd(3+), a different type of ligand whose recognition site on mGluR1alpha is distinct from the glutamate site, increased only [Ca(2+)](i) an

SUBMITTER: Tateyama M 

PROVIDER: S-EPMC1347971 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature