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After latching on to the phagophore, small active sites on the proteins glue the membranes together. These membranes fuse into one double-walled structure as components continue to be added to the autophagosome wall. The researchers found that the active sites on LC3B and GATE-16 each use a different mode of action, possibly explaining why both are necessary. They think that one of the proteins contributes to the elongation of the phagophore while the other may also function as the “latch” that seals the membrane shut when it reaches the proper size.