S-palmitoylation modulates ATG2-dependent non-vesicular lipid transport during starvation-induced autophagy

ABSTRACT: Lipid transfer proteins mediate the non-vesicular transport of lipids at membrane contact sites to regulate the lipid composition of organelle membranes. Despite significant recent advances in our understanding of the structural basis for lipid transfer, its functional regulation remains unclear. In this study, we report that S-palmitoylation modulates the cellular function of ATG2, a rod-like lipid transfer protein responsible for transporting phospholipids from the endoplasmic reticulum (ER) to phagophores during autophagosome formation. During starvation-induced autophagy, ATG2A undergoes overall depalmitoylation as the balance between the palmitoyltransferase ZDHHC11 and the depalmitoylase APT1 activities changes. Inhibition of ATG2A depalmitoylation leads to impaired autophagosome for

SUBMITTER: Wenhui Zheng 

PROVIDER: S-SCDT-10_1038-S44318-025-00410-7 | biostudies-other |

REPOSITORIES: biostudies-other