Metabotropic glutamate receptor type 1α and tubulin assemble into dynamic interacting complexes

Authors


Address correspondence and reprint requests to Francisco Ciruela, Departament de Bioquímica i Biologia Molecular, Universitat de Barcelona, Marti i Franquès 1, 08028 Barcelona, Spain. E-mail: recep@sun.bq.ub.es

Abstract

Metabotropic glutamate receptors (mGlu receptors) are coupled to G-protein second messenger pathways and modulate glutamate neurotransmission in the brain, where they are targeted to specific synaptic locations. Very recently, we identified tubulin as an interacting partner of the mGlu receptor in rat brain. Using BHK-570 cells permanently expressing the receptor we have shown that this interaction occurs predominantly with soluble tubulin, following its translocation to the plasma membrane. In addition, treatment of the cells with the agonist quisqualic acid induce tubulin depolimerization and its translocation to the plasma membrane. Immunofluorescence detection of both the receptor and tubulin in agonist-treated cells reveals a disruption of the microtubule network and an increased clustering of the receptor. Collectively these data demonstrate that the mGlu receptor interacts with soluble tubulin and that this association can take place at the plasma membrane.

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