Co-assembly of two GluR6 kainate receptor splice variants within a functional protein complex.
Neuron. 2005-08-01; 47(4): 555-566
DOI: 10.1016/j.neuron.2005.06.033
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1. Neuron. 2005 Aug 18;47(4):555-66.
Co-assembly of two GluR6 kainate receptor splice variants within a functional
protein complex.
Coussen F(1), Perrais D, Jaskolski F, Sachidhanandam S, Normand E, Bockaert J,
Marin P, Mulle C.
Author information:
(1)Laboratoire “Physiologie Cellulaire de la Synapse”, CNRS, UMR 5091, Institut
François Magendie, Université Bordeaux, 2, rue C. Saint-Saëns, 33077 Bordeaux
Cedex, France.
Kainate receptors (KAR) are composed of several distinct subunits and splice
variants, but the functional relevance of this diversity remains largely unclear.
Here we show that two splice variants of the GluR6 subunit, GluR6a and GluR6b,
which differ in their C-terminal domains, do not show distinct functional
properties, but coassemble as heteromers in vitro and in vivo. Using a proteomic
approach combining affinity purification and MALDI-TOF mass spectrometry, we
found that GluR6a and GluR6b interact with two distinct subsets of cytosolic
proteins mainly involved in Ca(2+) regulation of channel function and
intracellular trafficking. Guided by these results, we provide evidence that the
regulation of native KAR function by NMDA receptors depends on the
heteromerization of GluR6a and GluR6b and interaction of calcineurin with GluR6b.
Thus, GluR6a and GluR6b bring in close proximity two separate subsets of
interacting proteins that contribute to the fine regulation of KAR trafficking
and function.
DOI: 10.1016/j.neuron.2005.06.033
PMID: 16102538 [Indexed for MEDLINE]