Sergi Tosal-Castano, Carlotta Peselj, Verena Kohler, Lukas Habernig, Lisa Larsson Berglund, Mahsa Ebrahimi, F-Nora Vögtle, Johanna Höög, Claes Andréasson, Sabrina Büttner
Cell reports 2021 Jan 19Membrane contact sites facilitate the exchange of metabolites between organelles to support interorganellar communication. The nucleus-vacuole junctions (NVJs) establish physical contact between the perinuclear endoplasmic reticulum (ER) and the vacuole. Although the NVJ tethers are known, how NVJ abundance and composition are controlled in response to metabolic cues remains elusive. Here, we identify the ER protein Snd3 as central factor for NVJ formation. Snd3 interacts with NVJ tethers, supports their targeting to the contacts, and is essential for NVJ formation. Upon glucose exhaustion, Snd3 relocalizes from the ER to NVJs and promotes contact expansion regulated by central glucose signaling pathways. Glucose replenishment induces the rapid dissociation of Snd3 from the NVJs, preceding the slow disassembly of the junctions. In sum, this study identifies a key factor required for formation and regulation of NVJs and provides a paradigm for metabolic control of membrane contact sites. Copyright © 2020 The Author(s). Published by Elsevier Inc. All rights reserved.
Sergi Tosal-Castano, Carlotta Peselj, Verena Kohler, Lukas Habernig, Lisa Larsson Berglund, Mahsa Ebrahimi, F-Nora Vögtle, Johanna Höög, Claes Andréasson, Sabrina Büttner. Snd3 controls nucleus-vacuole junctions in response to glucose signaling. Cell reports. 2021 Jan 19;34(3):108637
PMID: 33472077
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