A novel binding site on the cryptic intervening domain is a motif-dependent regulator of O-GlcNAc transferase.

ABSTRACT: The modification of intracellular proteins with O-linked β- N -acetylglucosamine (O-GlcNAc) moieties is a highly dynamic process that spatiotemporally regulates nearly every important cellular program. Despite its significance, little is known about the substrate recognition and regulation modes of O-GlcNAc transferase (OGT), the primary enzyme responsible for O-GlcNAc addition. In this study, we have identified the intervening domain (Int-D), a poorly understood protein fold found only in metazoan OGTs, as a specific regulator of OGT protein-protein interactions and substrate modification. Utilizing an innovative proteomic peptide phage display (ProP-PD) coupled with structural, biochemical, and cellular characterizations, we discovered a novel peptide motif, employed by the Int-D

SUBMITTER: Blankenship C 

PROVIDER: S-EPMC9915769 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature