Abstract
Modulation of AMPA-type glutamate channels is important for synaptic plasticity. Here we provide physiological evidence that the activity of AMPA channels is regulated by protein phosphatase 1 (PP-1) in neostriatal neurons and identify two distinct molecular mechanisms of this regulation. One mechanism involves control of PP-1 catalytic activity by DARPP-32, a dopamine- and cAMP-regulated phosphoprotein highly enriched in neostriatum. The other involves binding of PP-1 to spinophilin, a protein that colocalizes PP-1 with AMPA receptors in postsynaptic densities. The results suggest that regulation of anchored PP-1 is important for AMPA-receptor-mediated synaptic transmission and plasticity.
Original language | English |
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Pages (from-to) | 13-17 |
Number of pages | 5 |
Journal | Nature Neuroscience |
Volume | 2 |
Issue number | 1 |
DOIs | |
Publication status | Published - Jan 1999 |
ASJC Scopus subject areas
- Neuroscience(all)