KDEL receptor regulates secretion by lysosome relocation- and autophagy-dependent modulation of lipid-droplet turnover

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Miniatura
Fecha
2019-12
Autores
Tapia, Diego
Jiménez, Tomás
Zamora, Constanza
Espinoza, Javier
Rizzo, Riccardo
González-Cárdenas, Alexis
Fuentes, Danitza
Hernández, Sergio
Cavieres, Viviana A.
Soza, Andrea
Profesor/a Guía
Facultad/escuela
Idioma
en
Título de la revista
ISSN de la revista
Título del volumen
Editor
Nature Publishing Group
Nombre de Curso
Licencia CC
Atribución 4.0 Internacional (CC BY 4.0)
Licencia CC
https://creativecommons.org/licenses/by/4.0/deed.es
Resumen
Inter-organelle signalling has essential roles in cell physiology encompassing cell metabolism, aging and temporal adaptation to external and internal perturbations. How such signalling coordinates different organelle functions within adaptive responses remains unknown. Membrane traffic is a fundamental process in which membrane fluxes need to be sensed for the adjustment of cellular requirements and homeostasis. Studying endoplasmic reticulum-to-Golgi trafficking, we found that Golgi-based, KDEL receptor-dependent signalling promotes lysosome repositioning to the perinuclear area, involving a complex process intertwined to autophagy, lipid-droplet turnover and Golgi-mediated secretion that engages the microtubule motor protein dynein-LRB1 and the autophagy cargo receptor p62/SQSTM1. This process, here named ‘traffic-induced degradation response for secretion’ (TIDeRS) discloses a cellular mechanism by which nutrient and membrane sensing machineries cooperate to sustain Golgi-dependent protein secretion. © 2019, The Author(s).
Notas
Indexación: Scopus
Palabras clave
Autophagy, Cell Line, Tumor, Cell Nucleus, Dyneins, Endoplasmic Reticulum, Golgi Apparatus, HeLa Cells, Humans, Lipid Droplets, Lysosomes, Microscopy, Electron, Transmission, Microtubules, Protein Transport, Receptors, Peptide, Sequestosome-1 Protein, Signal Transduction
Citación
Nature Communications Volume 10, Issue 11 December 2019 Article number 735
DOI
10.1038/s41467-019-08501-w
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