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The Journal of Neuroscience, November 28, 2007, 27(48):13273-13278; doi:10.1523/JNEUROSCI.3334-07.2007

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Brief Communications
Characterization of the Role of Microtubule-Associated Protein 1B in Metabotropic Glutamate Receptor-Mediated Endocytosis of AMPA Receptors in Hippocampus

Genoveva Davidkova¹ and Reed C. Carroll¹

¹Dominick P. Purpura Department of Neuroscience, Albert Einstein College of Medicine, Bronx, New York 10461

Correspondence should be addressed to Genoveva Davidkova at her present address: The Scripps Research Institute, MIND, 10550 North Torrey Pines Road, SP30-2120, La Jolla, CA 92037. Email: gdavidko{at}scripps.edu

The mGluR-dependent endocytosis of AMPA receptors (AMPARs) in the CA1 region is protein synthesis dependent. However, why this form of trafficking, and not that mediated by NMDA receptor activation, is dependent on protein translation is unclear. Here we have studied the contribution of the cytoskeletal microtubule-associated protein 1B (MAP1B) to the pathway-specific internalization of AMPARs. Treatments of cultured neurons with 3,4-dihydroxyphenylglycol (DHPG) or NMDA, both of which drive AMPAR endocytosis, caused a translation-dependent increase in the dendritic levels of MAP1B protein. Although interfering with protein synthesis using short interfering RNA (siRNA) to eEF2 kinase (eukaryotic elongation factor 2 kinase) blocked the dendritic MAP1B increase by both pathways, it selectively blocked the DHPG- and not the NMDA-induced AMPAR endocytosis. In support of MAP1B synthesis contributing to metabotropic glutamate receptor (mGluR)-mediated AMPAR endocytosis, siRNA against MAP1B in CA1 cultured neurons specifically blocked the DHPG-induced AMPAR internalization. Previous studies suggest a direct interaction between MAP1B and the AMPAR-binding protein GRIP1. Biochemical studies establish that MAP1B associates with GRIP1 and forms a complex with GluR2 in vivo in rat hippocampus. Furthermore, the interaction between MAP1B and GRIP1 increased significantly in acute slices after treatment with DHPG and not NMDA. Together, these findings suggest that MAP1B plays a selective role in the DHPG-induced endocytosis of AMPARs, perhaps through its interaction with GRIP1.

Key words: microtubule-associated protein 1B (MAP1B); GRIP; AMPA receptor endocytosis; metabotropic glutamate receptor-dependent LTD; NMDA receptor-dependent LTD; eukaryotic elongation factor 2 kinase (eEF2k); dendritic protein synthesis

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Received July 23, 2007; revised Oct. 12, 2007; accepted Oct. 22, 2007.

Correspondence should be addressed to Genoveva Davidkova at her present address: The Scripps Research Institute, MIND, 10550 North Torrey Pines Road, SP30-2120, La Jolla, CA 92037. Email: gdavidko{at}scripps.edu

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