Insights into the regulation of CHIP E3 ligase-mediated ubiquitination of neuronal protein BNIP-H.

ABSTRACT: BCL2/adenovirus E1B 19-kDa protein-interacting protein 2 homolog (BNIP-H or Caytaxin), a pivotal adaptor protein that facilitates cerebellar cortex growth and synaptic transmission, is posttranslationally modified to regulate neuronal function. This study reports the ubiquitination of BNIP-H by Carboxyl terminus of Hsc70-Interacting Protein (CHIP), a U-box containing E3 ligase that is also regulated via autoubiquitination. Specifically, it was observed that CHIP autoubiquitinated itself primarily at Lys23 and Lys31 in vitro. Mutation of these residues shows the autoubiquitination of successive lysines of CHIP. In total, nine lysines on CHIP were identified as the autoubiquitination sites, the collective mutation of which almost completely terminated its autoubiquitination. Ad

SUBMITTER: Shankar S 

PROVIDER: S-EPMC11658413 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature