Arginyltransferase 1 modulates p62-driven autophagy via mTORC1/AMPk signaling.

ABSTRACT:

Background

Arginyltransferase (Ate1) orchestrates posttranslational protein arginylation, a pivotal regulator of cellular proteolytic processes. In eukaryotic cells, two interconnected systems-the ubiquitin proteasome system (UPS) and macroautophagy-mediate proteolysis and cooperate to maintain quality protein control and cellular homeostasis. Previous studies have shown that N-terminal arginylation facilitates protein degradation through the UPS. Dysregulation of this machinery triggers p62-mediated autophagy to ensure proper substrate processing. Nevertheless, how Ate1 operates through this intricate mechanism remains elusive.

Methods

We investigated Ate1 subcellular distribution through confocal microscopy and biochemical assays using cells transiently or stably expressin

SUBMITTER: Bonnet LV 

PROVIDER: S-EPMC10832197 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature