Agonist-independent activation of metabotropic glutamate receptors by the intracellular protein Homer

Article Abstract:

It has been established that, in neurons, the constitutive activity of the metabotropic glutamate receptors mGluR1a and mGluR5 is determined by Homer proteins, which bind directly to the carboxy-terminal intracellular domains of the receptors. This work is consistent with earlier work showing that H1a does not have an impact on membrane localization of mGluR1a and mGluR5.

Glutamate, Protein binding

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Functional coupling between ryanodine receptors and L-type calcium channels in neurons

Article Abstract:

The stimulation of the type-1 metabotropic glutamate receptor (mGluR1) induces a tight functional coupling between ryanodine receptors and L-type calcium channels in neurons. The stimulation of mGluR1 facilitates L-type calcium channel activity. The stimulation of channel activity is independent of inositol 1,4,5-trisphosphate and typical protein kinases, and is mimicked by caffeine. Ryanodine inhibits both the mGluR1 and caffeine-induced increase in L-type calcium channels in neurons.

Analysis, Physiological aspects, Calcium channels, Neurons

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Homer: a protein that selectively binds metabotropic glutamate receptors

Article Abstract:

The PDZ proteins are a family of proteins that contain modular PDZ domains and interact with synaptic ionotropic glutamate receptors and ion channels. A new dendritic protein called Homer is described, which seems to be representative of a novel family. Unlike members of the PDZ family, Homer has a single, PDZ-like domain and binds specifically to the carboxy terminus of phosphoinositide-linked metabotropic glutamate receptors. The gene's expression is also regulated as an immediate early gene and is dynamically responsive to physiological synaptic activity, particularly during cortical development.

Membrane proteins

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