AMPylation Regulates 5'-3' Exonuclease PLD3 Processing.

ABSTRACT: The 5'-3' exonuclease phospholipase D3 (PLD3) is a single-pass transmembrane protein undergoing sequential post-translational modifications by N-glycosylation, AMPylation, and proteolytic cleavage. The substrates of PLD3 5'-3' exonuclease activity are single-stranded DNAs and RNAs, which act as ligands for Toll-like receptors and trigger a downstream proinflammatory response. Although PLD3 has primarily been studied in immune cells, recent findings indicate its enrichment in neurons, where it plays a role in regulating axonal fitness in Alzheimer's disease. However, the regulatory mechanisms governing the proteolytic processing of PLD3 into its catalytically active soluble form and its functional roles in both immune and neuronal cells remain unclear. Here, we describe the functional impli

SUBMITTER: Hoffmann L 

PROVIDER: S-EPMC12494813 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature