Homotypic SCOTIN assemblies form ER-endosome membrane contacts and regulate endosome dynamics
SCIE
SCOPUS
- Title
- Homotypic SCOTIN assemblies form ER-endosome membrane contacts and regulate endosome dynamics
- Authors
- HYERI, YUN; Minkyo Jung; HOJIN, LEE; Sungjin Jung; KIM, TAEHYEON; KIM, NARI; PARK, SEUNG YEOL; KIM, WON JONG; Ji Young Mun; YOO, JOO YEON
- Date Issued
- 2023-08
- Publisher
- Nature Publishing Group
- Abstract
- The ER regulates the spatiotemporal organization of endolysosomal systems by membrane contact. In addition to tethering via heterotypic interactions on both organelles, we present a novel ER-endosome tethering mechanism mediated by homotypic interactions. The single-pass transmembrane protein SCOTIN is detected in the membrane of the ER and endosomes. In SCOTIN-knockout (KO) cells, the ER-late endosome contacts are reduced, and the perinuclear positioning of endosomes is disturbed. The cytosolic proline-rich domain (PRD) of SCOTIN forms homotypic assemblies in vitro and is necessary for ER-endosome membrane tethering in cells. A region of 28 amino acids spanning 150–177 within the SCOTIN PRD is essential to elicit membrane tethering and endosomal dynamics, as verified by reconstitution in SCOTIN-KO cells. The assembly of SCOTIN (PRD) is sufficient to mediate membrane tethering, as purified SCOTIN (PRD), but not SCOTIN (PRDΔ150-177), brings two different liposomes closer in vitro. Using organelle-specific targeting of a chimeric PRD domain shows that only the presence on both organellar membranes enables the ER-endosome membrane contact, indicating that the assembly of SCOTIN on heterologous membranes mediates organelle tethering. © 2023 The Authors. Published under the terms of the CC BY NC ND 4.0 license.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/120541
- DOI
- 10.15252/embr.202256538
- ISSN
- 1469-221X
- Article Type
- Article
- Citation
- EMBO Reports, vol. 24, no. 8, 2023-08
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- There are no files associated with this item.
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