Abstract
Autophagy and endocytosis are two evolutionarily conserved catabolic processes that comprise vesicle trafficking events for the clearance of the sequestered intracellular and extracellular cargo. Both start differently but end in the same compartment, the lysosome. Mounting evidences from the last years have established the involvement of proteins sensitive to intracellular Ca2+ in the control of the early autophagic steps and in the traffic of autophagic, endocytic and lysosomal vesicles. However, this knowledge is based on dispersed outcomes that do not set up a consensus model of the Ca2+-dependent control of autophagy and endocytosis. Here, we will provide a critical synopsis of insights from the last decade on the involvement of Ca2+-sensor proteins in the activation of autophagy and in fusion events of endocytic vesicles, autophagosomes and lysosomes.
Highlights
Lysosomes are ubiquitous organelles that degrade material sequestered by two main dynamic processes: autophagy and endocytosis
While there are no experimental evidences for a direct involvement of the two other isoforms in autophagy, recent data have shown that TRPML3 is localized on autophagosomal membrance, where it induces autophagy under stress conditions [105, 118], and at the plasma membrane and early endosomal membranes, where it inhibits endocytosis [118, 119]
Its effect on autophagy occurs both at the level of the signalling pathways that initiate it or, later, when autophagosomes fuse with endolysosomal compartments
Summary
Lysosomes are ubiquitous organelles that degrade material sequestered by two main dynamic processes: autophagy and endocytosis. Starvation releases Beclin 1 from the complex with IP3R/Bcl-2 [54, 55] and this dissociation, which is a basic condition to activate autophagy, occurs when Beclin 1 is phosphorylated by the death-associated protein kinase (DAPK) [56].
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