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Abstract
An increasing body of research on autophagy provides overwhelming evidence for its
connection to diverse biological functions and human diseases. Beclin 1, the first
mammalian autophagy protein to be described, appears to act as a nexus point between
autophagy, endosomal, and perhaps also cell death pathways. Beclin 1 performs these
roles as part of a core complex that contains vacuolar sorting protein 34 (VPS34),
a class III phosphatidylinositol-3 kinase. The precise mechanism of Beclin 1-mediated
regulation of these cellular functions is unclear, but substantial progress has recently
been made in identifying new players and their functions in Beclin 1-VSP34 complexes.
Here we review emerging studies that are beginning to unveil the physiological functions
of Beclin 1-VPS34 in the central control of autophagic activity and other trafficking
events through the formation of distinct Beclin 1-VPS34 protein complexes.
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