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Coordination of autophagosome-lysosome fusion and transport by a Klp98A-Rab14 complex in Drosophila.
Mauvezin, Caroline; Neisch, Amanda L; Ayala, Carlos I; Kim, Jung; Beltrame, Abigail; Braden, Christopher R; Gardner, Melissa K; Hays, Thomas S; Neufeld, Thomas P.
Afiliación
  • Mauvezin C; Department of Genetics, Cell Biology and Development, 6-160 Jackson Hall, 321 Church St. SE, University of Minnesota, Minneapolis, MN 55455, USA.
  • Neisch AL; Department of Genetics, Cell Biology and Development, 6-160 Jackson Hall, 321 Church St. SE, University of Minnesota, Minneapolis, MN 55455, USA.
  • Ayala CI; Department of Genetics, Cell Biology and Development, 6-160 Jackson Hall, 321 Church St. SE, University of Minnesota, Minneapolis, MN 55455, USA.
  • Kim J; Department of Genetics, Cell Biology and Development, 6-160 Jackson Hall, 321 Church St. SE, University of Minnesota, Minneapolis, MN 55455, USA.
  • Beltrame A; Department of Genetics, Cell Biology and Development, 6-160 Jackson Hall, 321 Church St. SE, University of Minnesota, Minneapolis, MN 55455, USA.
  • Braden CR; Department of Genetics, Cell Biology and Development, 6-160 Jackson Hall, 321 Church St. SE, University of Minnesota, Minneapolis, MN 55455, USA.
  • Gardner MK; Department of Genetics, Cell Biology and Development, 6-160 Jackson Hall, 321 Church St. SE, University of Minnesota, Minneapolis, MN 55455, USA.
  • Hays TS; Department of Genetics, Cell Biology and Development, 6-160 Jackson Hall, 321 Church St. SE, University of Minnesota, Minneapolis, MN 55455, USA.
  • Neufeld TP; Department of Genetics, Cell Biology and Development, 6-160 Jackson Hall, 321 Church St. SE, University of Minnesota, Minneapolis, MN 55455, USA neufe003@umn.edu.
J Cell Sci ; 129(5): 971-82, 2016 Mar 01.
Article en En | MEDLINE | ID: mdl-26763909
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 new 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 towards 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 and 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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cinesinas / Proteínas de Unión al GTP rab / Proteínas de Drosophila / Drosophila melanogaster / Autofagosomas / Lisosomas Límite: Animals Idioma: En Revista: J Cell Sci Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cinesinas / Proteínas de Unión al GTP rab / Proteínas de Drosophila / Drosophila melanogaster / Autofagosomas / Lisosomas Límite: Animals Idioma: En Revista: J Cell Sci Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido