Phosphorylation regulates calpain-mediated truncation of glutamate ionotropic receptors

Brain Res. 1998 Jun 22;797(1):154-8. doi: 10.1016/s0006-8993(98)00433-8.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Calpain / antagonists & inhibitors
  • Calpain / metabolism*
  • Enzyme Inhibitors / pharmacology
  • Molecular Weight
  • Neuronal Plasticity / physiology
  • Phosphorylation
  • Rats
  • Rats, Sprague-Dawley
  • Receptors, AMPA / chemistry
  • Receptors, AMPA / metabolism*
  • Telencephalon / chemistry
  • Telencephalon / enzymology

Substances

  • Enzyme Inhibitors
  • Receptors, AMPA
  • Calpain
  • glutamate receptor ionotropic, AMPA 2
  • glutamate receptor ionotropic, AMPA 1