Ontology highlight
ABSTRACT:
SUBMITTER: Colledge M
PROVIDER: S-EPMC3963808 | biostudies-literature | 2003 Oct
REPOSITORIES: biostudies-literature
Colledge Marcie M Snyder Eric M EM Crozier Robert A RA Soderling Jacquelyn A JA Jin Yetao Y Langeberg Lorene K LK Lu Hua H Bear Mark F MF Scott John D JD
Neuron 20031001 3
PSD-95 is a major scaffolding protein of the postsynaptic density, tethering NMDA- and AMPA-type glutamate receptors to signaling proteins and the neuronal cytoskeleton. Here we show that PSD-95 is regulated by the ubiquitin-proteasome pathway. PSD-95 interacts with and is ubiquitinated by the E3 ligase Mdm2. In response to NMDA receptor activation, PSD-95 is ubiquitinated and rapidly removed from synaptic sites by proteasome-dependent degradation. Mutations that block PSD-95 ubiquitination prev ...[more]