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TitleMembrane constriction and thinning by sequential ESCRT-III polymerization.
Journal, issue, pagesNat Struct Mol Biol, Vol. 27, Issue 4, Page 392-399, Year 2020
Publish dateApr 6, 2020
AuthorsHenry C Nguyen / Nathaniel Talledge / John McCullough / Abhimanyu Sharma / Frank R Moss / Janet H Iwasa / Michael D Vershinin / Wesley I Sundquist / Adam Frost /
PubMed AbstractThe endosomal sorting complexes required for transport (ESCRTs) mediate diverse membrane remodeling events. These typically require ESCRT-III proteins to stabilize negatively curved membranes; ...The endosomal sorting complexes required for transport (ESCRTs) mediate diverse membrane remodeling events. These typically require ESCRT-III proteins to stabilize negatively curved membranes; however, recent work has indicated that certain ESCRT-IIIs also participate in positive-curvature membrane-shaping reactions. ESCRT-IIIs polymerize into membrane-binding filaments, but the structural basis for negative versus positive membrane remodeling by these proteins remains poorly understood. To learn how certain ESCRT-IIIs shape positively curved membranes, we determined structures of human membrane-bound CHMP1B-only, membrane-bound CHMP1B + IST1, and IST1-only filaments by cryo-EM. Our structures show how CHMP1B first polymerizes into a single-stranded helical filament, shaping membranes into moderate-curvature tubules. Subsequently, IST1 assembles a second strand on CHMP1B, further constricting the membrane tube and reducing its diameter nearly to the fission point. Each step of constriction thins the underlying bilayer, lowering the barrier to membrane fission. Our structures reveal how a two-component, sequential polymerization mechanism drives membrane tubulation, constriction and bilayer thinning.
External linksNat Struct Mol Biol / PubMed:32251413 / PubMed Central
MethodsEM (helical sym.)
Resolution3.1 - 7.2 Å
Structure data

20588

6tz4

EMDB-20588, PDB-6tz4:
CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (right-handed)
Method: EM (helical sym.) / Resolution: 3.2 Å

20589

6tz5

EMDB-20589, PDB-6tz5:
CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (left-handed)
Method: EM (helical sym.) / Resolution: 3.1 Å

20590

6tz9

EMDB-20590, PDB-6tz9:
CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B only
Method: EM (helical sym.) / Resolution: 6.2 Å

20591

6tza

EMDB-20591, PDB-6tza:
CryoEM reconstruction of ESCRT-III filament composed of IST1 NTD R16E K27E double mutant
Method: EM (helical sym.) / Resolution: 7.2 Å

Source
  • homo sapiens (human)
KeywordsLIPID BINDING PROTEIN / membrane remodeling / membrane-bound protein filament / ESCRT-III

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