Profilin II regulates the exocytosis of kainate glutamate receptors
J. Biol. Chem.. 2010-10-11; 285(51): 40060-40071
DOI: 10.1074/jbc.M110.140442
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1. J Biol Chem. 2010 Dec 17;285(51):40060-71. doi: 10.1074/jbc.M110.140442. Epub
2010 Oct 11.
Profilin II regulates the exocytosis of kainate glutamate receptors.
Mondin M(1), Carta M, Normand E, Mulle C, Coussen F.
Author information:
(1)Laboratoire Physiologie Cellulaire de la Synapse, CNRS UMR 5091, University of
Bordeaux, 146 rue Léo Saignat, 33077 Bordeaux Cedex, France.
The trafficking of ionotropic glutamate receptors to and from synaptic sites is
regulated by proteins that interact with their cytoplasmic C-terminal domain.
Profilin IIa (PfnIIa), an actin-binding protein expressed in the brain and
recruited to synapses in an activity-dependent manner, was shown previously to
interact with the C-terminal domain of the GluK2b subunit splice variant of
kainate receptors (KARs). Here, we characterize this interaction and examine the
role of PfnIIa in the regulation of KAR trafficking. PfnIIa directly and
specifically binds to the C-terminal domain of GluK2b through a diproline motif.
Expression of PfnIIa in transfected COS-7 cells and in cultured hippocampal
neurons from PfnII-deficient mice decreases the level of extracellular of
homomeric GluK2b as well as heteromeric GluK2a/GluK2b KARs. Our data suggest a
novel mechanism by which PfnIIa exerts a dual role on the trafficking of KARs, by
a generic inhibition of clathrin-mediated endocytosis through its interaction
with dynamin-1, and by controlling KARs exocytosis through a direct and specific
interaction with GluK2b.
DOI: 10.1074/jbc.M110.140442
PMCID: PMC3000988
PMID: 20937818 [Indexed for MEDLINE]