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

• Published in: Journal of neurochemistry 2001-02, Vol.76 (3), p.750-757
• Main Authors: Ciruela, Francisco, McIlhinney, R. A. Jeffrey
• Format: Article
• Language: English
• Subjects: Biological and medical sciences; Cell interactions, adhesion; Fundamental and applied biological sciences. Psychology; mGlu1α receptor; Molecular and cellular biology; tubulin‐interaction‐cell surface
• ISSN: 0022-3042; 1471-4159
• DOI: 10.1046/j.1471-4159.2001.00099.x

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 mGlu1α 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 mGlu1α receptor interacts with soluble tubulin and that this association can take place at the plasma membrane.