Regulation of PP1 interaction with I-2, neurabin, and F-actin.

ABSTRACT: Reversible phosphorylation is a fundamental regulatory mechanism required for many biological processes and is coordinated by the opposing actions of protein kinases and phosphatases. Protein phosphatase 1 (PP1) is a major protein phosphatase that plays an important role in many fundamental physiological processes including synaptic transmission and memory formation. Here we investigate the regulation of PP1 by prominent signaling proteins and synaptic scaffolds including GSK3β, inhibitor-2 (I-2), neurabin (Nrb), and actin. While GSK3β is known to regulate PP1 via phosphorylation of the PP1-binding protein I-2, we found that GSK3β directly regulates PP1 via inhibitory phosphorylation in neurons. Additionally, using bioluminescence resonance energy transfer (BRET), we found that GSK3β alter

SUBMITTER: Foley K 

PROVIDER: S-EPMC10038014 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature