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

Diego Tapia, Tomás Jiménez, Constanza Zamora, Javier Espinoza, Riccardo Rizzo, Alexis González-Cárdenas, Danitza Fuentes, Sergio Hernández, Viviana A. Cavieres, Andrea Soza, Fanny Guzmán, Gloria Arriagada, María Isabel Yuseff, Gonzalo A. Mardones, Patricia V. Burgos, Alberto Luini, Alfonso González and Jorge Cancino ()
Additional contact information
Diego Tapia: Universidad San Sebastián
Tomás Jiménez: Universidad San Sebastián
Constanza Zamora: Universidad San Sebastián
Javier Espinoza: Universidad Andrés Bello
Riccardo Rizzo: Istituto di Biochimica delle Proteine (IBP)
Alexis González-Cárdenas: Universidad Austral de Chile
Danitza Fuentes: Pontificia Universidad Católica de Chile
Sergio Hernández: Universidad San Sebastián
Viviana A. Cavieres: Universidad San Sebastián
Andrea Soza: Universidad San Sebastián
Fanny Guzmán: Fraunhofer Chile Research
Gloria Arriagada: Universidad Andrés Bello
María Isabel Yuseff: Pontificia Universidad Católica de Chile
Gonzalo A. Mardones: Universidad San Sebastián
Patricia V. Burgos: Universidad San Sebastián
Alberto Luini: Istituto di Biochimica delle Proteine (IBP)
Alfonso González: Universidad San Sebastián
Jorge Cancino: Universidad San Sebastián

Nature Communications, 2019, vol. 10, issue 1, 1-17

Abstract: Abstract 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.

Date: 2019
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DOI: 10.1038/s41467-019-08501-w

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