Acid sphingomyelinase recruits palmitoylated CD36 to membrane rafts and enhances lipid uptake.

ABSTRACT: CD36 palmitoylation increases its membrane localization and is required for CD36-mediated uptake of oxidized low-density lipoprotein (oxLDL). Acid sphingomyelinase (ASMase) is transported to the plasma membrane, where it promotes lipid raft clustering, facilitating membrane protein anchoring for biological functions. We investigated the effects of oxLDL on CD36 palmitoylation and explored the role of ASMase in CD36 membrane translocation. We found that oxLDL increased CD36 palmitoylation and drives its intracellular trafficking from the endoplasmic reticulum to the plasma membrane lipid rafts in macrophages. Affinity purification followed by mass spectrometry analysis identified CD36 bound to ASMase in the plasma membrane. The CD36/ASMase binding was enhanced by oxLDL treatment. Genetic ab

SUBMITTER: Ding M 

PROVIDER: S-EPMC12180984 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature