PDZD8 interacts with Protrudin and Rab7 at ER-late endosome membrane contact sites associated with mitochondria

Yael Elbaz-Alon (), Yuting Guo, Nadav Segev, Michal Harel, Daniel E. Quinnell, Tamar Geiger, Ori Avinoam, Dong Li and Jodi Nunnari ()
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Yael Elbaz-Alon: University of California Davis
Yuting Guo: Chinese Academy of Sciences
Nadav Segev: Weizmann Institute of Science
Michal Harel: Tel-Aviv University
Daniel E. Quinnell: University of California Davis
Tamar Geiger: Tel-Aviv University
Ori Avinoam: Weizmann Institute of Science
Dong Li: Chinese Academy of Sciences
Jodi Nunnari: University of California Davis

Nature Communications, 2020, vol. 11, issue 1, 1-14

Abstract: Abstract Endosomes are compositionally dynamic organelles that regulate signaling, nutrient status and organelle quality by specifying whether material entering the cells will be shuttled back to the cell surface or degraded by the lysosome. Recently, membrane contact sites (MCSs) between the endoplasmic reticulum (ER) and endosomes have emerged as important players in endosomal protein sorting, dynamics and motility. Here, we show that PDZD8, a Synaptotagmin-like Mitochondrial lipid-binding Proteins (SMP) domain-containing ER transmembrane protein, utilizes distinct domains to interact with Rab7-GTP and the ER transmembrane protein Protrudin and together these components localize to an ER-late endosome MCS. At these ER-late endosome MCSs, mitochondria are also recruited to form a three-way contact. Thus, our data indicate that PDZD8 is a shared component of two distinct MCSs and suggest a role for SMP-mediated lipid transport in the regulation of endosome function.

Date: 2020
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DOI: 10.1038/s41467-020-17451-7

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