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, Jodi Nunnari

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Article number3645
JournalNature Communications
Volume11
Issue number1
DOIs
StatePublished - 1 Dec 2020

Funding

FundersFunder number
Joseph and Bessie Feinberg Foundation
National Institutes of Health
National Institute of General Medical SciencesR01GM126081, R37GM097432
National Natural Science Foundation of China91754202
Chinese Academy of SciencesXDB19040101
Ministry of Science and Technology of the People's Republic of China
Ministry of Science and Technology2016YFA0500203

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