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    The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization

    Year: 2021

    Journal: BMC Biol., Volume 19, APR 8

    Authors: Alqabandi, Maryam; de Franceschi, Nicola; Maity, Sourav; Miguet, Nolwenn; Bally, Marta; Roos, Wouter H.; Weissenhorn, Winfried; Bassereau, Patricia; Mangenot, Stephanie

    Organizations: FINOVI; ANR [ANR-14-CE09-000301]; Institut Universitaire de France (IUF); sorbonne Universite; platforms of the Grenoble Instruct-ERIC center (ISBG) within the Grenoble Partnership for Structural Biology (PSB) [UMS 3518]; FRISBI [ANR-10-INBS-05-02]; GRAL, a project of the University Grenoble Alpes graduate school (Ecole Universitaire de Recherche) CBH-EUR-GS [ANR17-EURE-0003]; NWO VIDI grant; EU Marie Curie fellowship [INTERACT 751404]; Universite Pierre et Marie Curie/sorbonne Universite, Doctoral school Physique en Ile de France [ED-564]; Fondation pour la Recherche Medicale; Institute Curie; Fondation pour la Recherche Medicale a EMBO nonstipendiary long-term fellowship [ALTF 818-2016]; European Union [751715]; Labex CelTisPhyBio [ANR-11-798 LABX0038]; Paris Sciences et Lettres [ANR-10-IDEX-000102]

    Keywords: Endosomal sorting complexes  Required for Transport (ESCRT); Reconstituted system; Bottom up approach; Lipid-protein interactions; Membrane; Mechanical properties; Giant unilamellar vesicles (GUV); Micropipette; Atomic force microscopy (AFM)

    Background ESCRT-III proteins are involved in many membrane remodeling processes including multivesicular body biogenesis as first discovered in yeast. In humans, ESCRT-III CHMP2 exists as two isoforms, CHMP2A and CHMP2B, but their physical characteristics have not been compared yet. Results Here, we use a combination of techniques on biomimetic systems and purified proteins to study their affinity and effects on membranes. We establish that CHMP2B binding is enhanced in the presence of PI(4,5)P2 lipids. In contrast, CHMP2A does not display lipid specificity and requires CHMP3 for binding significantly to membranes. On the micrometer scale and at moderate bulk concentrations, CHMP2B forms a reticular structure on membranes whereas CHMP2A (+CHMP3) binds homogeneously. Thus, CHMP2A and CHMP2B unexpectedly induce different mechanical effects to membranes: CHMP2B strongly rigidifies them while CHMP2A (+CHMP3) has no significant effect. Conclusions We therefore conclude that CHMP2B and CHMP2A exhibit different mechanical properties and might thus contribute differently to the diverse ESCRT-III-catalyzed membrane remodeling processes.
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