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- W2292859969 abstract "Degradation of cellular material by autophagy is essential for cell survival and homeostasis, and requires intracellular transport of autophagosomes to encounter acidic lysosomes through unknown mechanisms. Here we identify the PX domain-containing kinesin Klp98A as a novel regulator of autophagosome formation, transport and maturation in Drosophila. Depletion of Klp98A caused abnormal clustering of autophagosomes and lysosomes at the cell center and reduced the formation of starvation-induced autophagic vesicles. Reciprocally, overexpression of Klp98A redistributed autophagic vesicles toward the cell periphery. These effects were accompanied by reduced autophagosome-lysosome fusion and autophagic degradation. In contrast, depletion of the conventional kinesin heavy chain caused a similar mislocalization of autophagosomes without perturbing their fusion with lysosomes, indicating that vesicle fusion and localization are separable, independent events. Klp98A-mediated fusion required the endolysosomal GTPase Rab14, which interacted and colocalized with Klp98A and required Klp98A for normal localization. Thus, Klp98A coordinates the movement and fusion of autophagic vesicles by regulating their positioning and interaction with the endolysosomal compartment." @default.
- W2292859969 created "2016-06-24" @default.
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- W2292859969 date "2016-01-01" @default.
- W2292859969 modified "2023-10-12" @default.
- W2292859969 title "Coordination of autophagosome-lysosome fusion and transport by a Klp98A-Rab14 complex" @default.
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- W2292859969 doi "https://doi.org/10.1242/jcs.175224" @default.
- W2292859969 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4813314" @default.
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