Phosphorylation regulates calpain-mediated truncation of glutamate ionotropic receptors.
Pre-incubation of synaptic membranes with phosphatase inhibitors significantly reduces the extent of calpain-mediated truncation of both GluR1 and NR2 subunits of AMPA and NMDA receptors, respectively. The same treatment did not modify calpain-mediated truncation of spectrin. These results might have important implications for mechanisms of synaptic plasticity as the balance of kinase/phosphatase activity and calpain has been proposed to regulate synaptic efficacy at glutamatergic synapses.
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Neuroscience Program, USC, Los Angeles, CA 90089-2520, USA.
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Baudry
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D000818:Animals; D002154:Calpain / Q000037:antagonists & inhibitors / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D008970:Molecular Weight; D009473:Neuronal Plasticity / Q000502:physiology; D010766:Phosphorylation; D051381:Rats; D017207:Rats, Sprague-Dawley; D018091:Receptors, AMPA / Q000737:chemistry / Q000378:metabolism*; D013687:Telencephalon / Q000737:chemistry / Q000201:enzymology
D002154:Calpain; D004791:Enzyme Inhibitors; D018091:Receptors, AMPA; C104722:glutamate receptor ionotropic, AMPA 2