Metabotropic glutamate receptor 4 interacts with microtubule-associated protein 1B.
The metabotropic glutamate receptor 4 (mGluR4) is a G-protein-coupled receptor that mediates inhibition of neurotransmitter release. Here, we used a proteomic approach to identify novel interaction partners of mGluR4 and report that the cytoplasmic C-terminal tail of mGluR4 interacts with microtubule-associated protein 1B (MAP1B). Binding of MAP1B to mGluR4 is inhibited by Ca(2+)/calmodulin, and MAP1B and mGluR4 colocalize at excitatory synapses in cultured hippocampal neurons. Thus, MAP1B might be implicated in the synaptic trafficking and/or regulation of mGluR4.
Department of Neurochemistry, Max-Planck-Institute for Brain Research, Deutschordenstrasse 46, 60528 Frankfurt, Germany.
Anina
A
Moritz
Astrid
A
Scheschonka
Tobias
T
Beckhaus
Michael
M
Karas
Heinrich
H
Betz
D000595:Amino Acid Sequence; D000818:Animals; D002147:Calmodulin / Q000378:metabolism; D051379:Mice; D008810:Mice, Inbred C57BL; D008817:Mice, Mutant Strains; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D025941:Protein Interaction Mapping; D040901:Proteomics / Q000379:methods; D051381:Rats; D017208:Rats, Wistar; D018094:Receptors, Metabotropic Glutamate / Q000378:metabolism*
D002147:Calmodulin; D008869:Microtubule-Associated Proteins; D018094:Receptors, Metabotropic Glutamate; C085284:microtubule-associated protein 1B; C108823:metabotropic glutamate receptor 4