期刊
NATURE CELL BIOLOGY
卷 7, 期 12, 页码 1179-1190出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb1325
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- Intramural NIH HHS Funding Source: Medline
- NIGMS NIH HHS [GM070902] Funding Source: Medline
- NIMH NIH HHS [F32MH65092, F32 MH065092] Funding Source: Medline
Appropriate trafficking and targeting of glutamate receptors (GIuRs) 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 G alpha i interaction domain, thus implicating G-protein signalling in the regulation of postsynaptic structure and trafficking of GluRs.
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