ISSN:
1471-4159
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Abstract : Metabotropic glutamate receptors (mGluRs) are coupled toG protein second messenger pathways and modulate glutamate neurotransmissionin the brain, where they are targeted to specific synaptic locations. As partof a strategy for defining the mechanisms for the specific targeting of mGluR1α, rat brain proteins which interact with the intracellular carboxyterminus of mGluR1 α have been characterized, using affinitychromatography on a glutathione S-transferase fusion protein thatcontains the last 86 amino acids of mGluR1 α. Three of the proteinsspecifically eluted from the affinity column yielded protein sequences, two ofwhich were identified as glyceraldehyde-3-phosphate dehydrogenase andβ-tubulin ; the other was an unknown protein. The identity of tubulin wasconfirmed by western immunoblotting. Using a solid-phase binding assay, themGluR1 α-tubulin interaction was shown to be direct, specific, andsaturable with a KD of 2.3 ± 0.4 μM. In addition, mGluR1 α, but not mGluR2/3 or mGluR4, could be coimmunoprecipitated from solubilized brain extracts with tubulin using anti-β-tubulin antibodies. However, mGluR1 α could not be coimmunoprecipitated with the tubulin binding protein gephyrin, nor could it be coimmunoprecipitated with PSD95. Collectively these data demonstrate that the last 86 amino acids of the carboxyl-terminal tail of mGluR1 α are sufficient to determine its interaction with tubulin and that there is an association of this receptor with tubulin in rat brain.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1046/j.1471-4159.1999.0720346.x
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