mPins modulates PSD-95 and SAP102 trafficking and influences NMDA receptor surface expression.
Nat Cell Biol. 2005-11-20; 7(12): 1179-1190
DOI: 10.1038/ncb1325
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Sans N(1), Wang PY, Du Q, Petralia RS, Wang YX, Nakka S, Blumer JB, Macara IG, Wenthold RJ.
Author information:
(1)Laboratory of Neurochemistry, National Institute on Deafness and Other
Communication Disorders, National Institutes of Health, Building 50, Room 4146,
50 South Drive, Bethesda, MD 20892-8027, USA.
Erratum in
Nat Cell Biol. 2006 Jan;8(1):100.
Appropriate trafficking and targeting of glutamate receptors (GluRs) to the
postsynaptic density is crucial for synaptic function. We show that mPins
(mammalian homologue of Drosophila melanogaster partner of inscuteable) interacts
with SAP102 and PSD-95 (two PDZ proteins present in neurons), and functions in
the formation of the NMDAR-MAGUK (N-methyl-D-aspartate
receptor-membrane-associated guanylate kinase) complex. mPins enhances
trafficking of SAP102 and NMDARs to the plasma membrane in neurons. Expression of
dominant-negative constructs and short-interfering RNA (siRNA)-mediated knockdown
of mPins decreases SAP102 in dendrites and modifies surface expression of NMDARs.
mPins changes the number and morphology of dendritic spines and these effects
depend on its Galphai interaction domain, thus implicating G-protein signalling
in the regulation of postsynaptic structure and trafficking of GluRs.