Toward the function of mammalian ATG12-ATG5-ATG16L1 complex in autophagy and related processes.
Alf Håkon LystadSven R CarlssonAnne SimonsenPublished in: Autophagy (2019)
The machinery that decorates autophagic membranes with lipid-conjugated LC3/GABARAP is not yet fully understood. We recently reported the purification of the full-length ATG12-ATG5-ATG16L1 complex, and in reconstitution experiments with purified ATG7, ATG3, and LC3/GABARAP in vitro, together with rescue experiments in knockout cells, important aspects of the complete lipidation reaction were revealed. Hitherto unobserved membrane-binding regions in ATG16L1 were found, contributing to properties that explain the crucial role of this protein in membrane targeting and LC3/GABARAP lipidation in macroautophagy/autophagy and other related processes.
Keyphrases
- cell death
- endoplasmic reticulum stress
- signaling pathway
- mass spectrometry
- induced apoptosis
- simultaneous determination
- liquid chromatography
- drug delivery
- cell cycle arrest
- single cell
- transcription factor
- cell proliferation
- fatty acid
- solid phase extraction
- binding protein
- amino acid
- tandem mass spectrometry
- high resolution mass spectrometry
- wild type