Differences in Src phosphorylation of PSD-93 and PSD-95 drive differences in scaffolding activity.
Ontology highlight
ABSTRACT: Scaffold proteins contain multiple binding modules that allow for co-localization of proteins that lack a direct interaction. Evolution resulted in different combinations of binding modules that rewired existing signal transduction pathways. The synaptic Membrane-Associated Guanylate Kinase (MAGuK) scaffold proteins post-synaptic density protein 93 (PSD-93) and post-synaptic density protein 95 (PSD-95) share the same organization of highly conserved binding domains connected by divergent linkers, which generates opposing functions in synaptic plasticity. Both are targets for tyrosine phosphorylation by Src kinase, but the extent and impacts of phosphorylation are poorly understood. Here, we characterized the in vitro phosphorylation of PSD-93 and PSD-95. Both were targeted at multiple site
SUBMITTER: Mindlin FA
PROVIDER: S-EPMC12820800 | biostudies-literature | 2026 Feb
REPOSITORIES: biostudies-literature
ACCESS DATA