Journal
JOURNAL OF CELL SCIENCE
Volume 132, Issue 4, Pages -Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.217968
Keywords
ESCRT; CHMP2B; Dendritic spine; GUV; Membrane fusion
Categories
Funding
- FINOVI
- ANR [ANR-14-CE09-0003-01]
- Institut Curie
- Fondation pour la Recherche Medicale [SPF20160936338]
- European Molecular Biology Organization (EMBO) non-stipendiary long term fellowship [ALTF 818-2016]
- European Union's Horizon 2020 research and innovation programme under the Marie Sklodowska-Curie Grant [751715]
- Universite Pierre et Marie Curie, doctoral school 'Physique en Ile de France' [ED-564]
- Fondation pour la Recherche Medicale
- Marie Curie Actions (MSCA) [751715] Funding Source: Marie Curie Actions (MSCA)
- Agence Nationale de la Recherche (ANR) [ANR-14-CE09-0003] Funding Source: Agence Nationale de la Recherche (ANR)
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Endosomal sorting complexes required for transport (ESCRT)-III family proteins catalyze membrane remodeling processes that stabilize and constrict membrane structures. It has been proposed that stable ESCRT-III complexes containing CHMP2B could establish diffusion barriers at the post-synaptic spine neck. In order to better understand this process, we developed a novel method based on fusion of giant unilamellar vesicles to reconstitute ESCRT-III proteins inside GUVs, from which membrane nanotubes are pulled. The new assay ensures that ESCRT-III proteins polymerize only when they become exposed to physiologically relevant membrane topology mimicking the complex geometry of post-synaptic spines. We establish that CHMP2B, both full-length and with a C-terminal deletion (Delta C), preferentially binds to membranes containing phosphatidylinositol 4,5-bisphosphate [PI(4,5) P2]. Moreover, we show that CHMP2B preferentially accumulates at the neck of membrane nanotubes, and provide evidence that CHMP2B-Delta C prevents the diffusion of PI(4,5) P2 lipids and membrane-bound proteins across the tube neck. This indicates that CHMP2B polymers formed at a membrane neck may function as a diffusion barrier, highlighting a potential important function of CHMP2B in maintaining synaptic spine structures.
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