Autophagy is a key proteostasis pathway that maintains cytoplasmic quality control by recycling damaged and/or superfluous cellular organelles and proteins, including many aggregation-prone proteins implicated in neurodegenerative diseases. Autophagy cargo is captured by phagophores, which form as outgrowths of the recycling endosome compartment. Phagophores grow around autophagy cargoes by extending “finger-like” membrane protrusions and are closed by components of the endosomal sorting complex required for transport (ESCRT) complex to form closed intermediate autophagic structures still attached to the recycling endosome, here termed “autophago-domes.” The Rubinsztein lab had shown previously that autophagosomes must be closed before subsequent release from the recycling endosome by dynamin 2 (DNM2). In this paper from Jennifer Palmer and colleagues in the Rubinsztein lab, researchers sought to identify the molecular mechanism that enables the coordination of autophagosome closure by the ESCRT complex and autophagosome release by DNM2. They identified that the Alzheimer’s disease-associated protein bridging integrator 1 (BIN1) is a critical mediator of this coordination. Prior to autophagosome closure, BIN1 is held at autophagosomes by ESCRT-III and inhibits DNM2. Once the autophagosome has closed and ESCRT-III disassembles, BIN1 is released, removing the inhibition of DNM2. This mechanism provides insight into the functional consequences of increased BIN1 expression, as this occurs in microglia with Alzheimer’s disease risk-associated polymorphisms. They found that the overexpression of BIN1 microglial isoforms inhibits DNM2-mediated autophagosome release and autophagic clearance. This provides a coherent explanation for the increased Alzheimer’s disease risk associated with BIN1, as impaired microglial autophagy alters phagocytosis and is associated with microglial senescence and neuroinflammation.