O-GlcNAcylation of ribosome-associated proteins is concomitant with translational reprogramming during proteotoxic stress.

ABSTRACT: Protein O-GlcNAc modification, similar to phosphorylation, supports cell survival by regulating key processes like transcription, cell division, trafficking, signaling, and stress tolerance. However, its role in protein homeostasis, particularly in protein synthesis, folding, and degradation, remains poorly understood. Our previous research shows that O-GlcNAc cycling enzymes associate with the translation machinery during protein synthesis and modify ribosomal proteins. Protein translation is closely linked to 26S proteasome activity, which recycles amino acids and clears misfolded proteins during stress, preventing aggregation and cell death. In this study, we demonstrate that pharmacological perturbation of the proteasome-like that used in cancer treatment- leads to the increased abunda

SUBMITTER: Zeidan Q 

PROVIDER: S-EPMC11567021 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature