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Intracellular membrane trafficking is essential for eukaryotic cell existence.Here, we show that RAB37, a small GTPase involved in vesicle transport, is a target of ATG5, a key protein required for autophagy.RAB37 activation through GTP binding recruits ATG5-12 to isolation membrane and promotes autophagosome formation.Mutation analysis reveals that GTP-bound RAB37 exhibits enhanced interactions with ATG5-12 and GDP-stabilized mutation impairs the interactions.