Figure 1.

Schematic depiction of ATG12–ATG5-ATG16L1 complex in solution, and bound to target membrane recruiting the ATG3–ATG8 conjugate. Regions of importance for the function of ATG16L1 are indicated. It is not known if the amphipathic α-helix (designated as ‘helix 2’) is present already in the soluble complex and interacts in the dimer (as found in crystal structures), or is formed only when the complex partially inserts into the membrane. The C terminus of ATG16L1 is thought to mediate specific membrane targeting, both through protein-protein interactions and through β-isoform-specific membrane binding.