- EMDB-28702: CryoEM reconstruction of membrane-bound, left-handed CHMP1B+IST1 ... -
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Basic information
Entry
Database: EMDB / ID: EMD-28702
Title
CryoEM reconstruction of membrane-bound, left-handed CHMP1B+IST1 filament with iodinated cholesterol probe
Map data
Left-handed, 17-subunit-per-turn, membrane-bound CHMP1B/IST1 with iodinated cholesterol.
Sample
Complex: Helical copolymer of CHMP1B and IST1 bound to a lipid membrane nanotube
Protein or peptide: CHMP1B
Protein or peptide: IST1
Keywords
ESCRT / brominated / lipid / membrane / MEMBRANE PROTEIN
Function / homology
Function and homology information
viral capsid secondary envelopment / MIT domain binding / abscission / amphisome membrane / multivesicular body-lysosome fusion / vesicle fusion with vacuole / ESCRT III complex disassembly / late endosome to lysosome transport / ESCRT III complex / kinetochore microtubule ...viral capsid secondary envelopment / MIT domain binding / abscission / amphisome membrane / multivesicular body-lysosome fusion / vesicle fusion with vacuole / ESCRT III complex disassembly / late endosome to lysosome transport / ESCRT III complex / kinetochore microtubule / endosome transport via multivesicular body sorting pathway / cytoskeleton-dependent cytokinesis / regulation of centrosome duplication / collateral sprouting / nuclear membrane reassembly / positive regulation of collateral sprouting / Sealing of the nuclear envelope (NE) by ESCRT-III / midbody abscission / multivesicular body sorting pathway / membrane coat / plasma membrane repair / membrane fission / late endosome to vacuole transport / multivesicular body membrane / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / multivesicular body assembly / regulation of mitotic spindle assembly / Flemming body / mitotic metaphase chromosome alignment / nucleus organization / viral budding via host ESCRT complex / autophagosome membrane / positive regulation of proteolysis / autophagosome maturation / endoplasmic reticulum-Golgi intermediate compartment / viral release from host cell / nuclear pore / multivesicular body / viral budding from plasma membrane / establishment of protein localization / kinetochore / autophagy / azurophil granule lumen / protein localization / protein transport / nuclear envelope / midbody / endosome membrane / cadherin binding / protein domain specific binding / cell division / lysosomal membrane / intracellular membrane-bounded organelle / centrosome / Neutrophil degranulation / protein-containing complex binding / chromatin / extracellular exosome / extracellular region / nucleoplasm / identical protein binding / plasma membrane / cytosol Similarity search - Function
Vacuolar protein sorting-associated protein Ist1 / Regulator of Vps4 activity in the MVB pathway / Vacuolar protein sorting-associated protein IST1-like / Snf7 family / Snf7 Similarity search - Domain/homology
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM117593
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM137109
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM082545
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM110772
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM089740
United States
Howard Hughes Medical Institute (HHMI)
United States
Chan Zuckerberg Initiative
United States
Citation
Journal: Nat Struct Mol Biol / Year: 2020 Title: Membrane constriction and thinning by sequential ESCRT-III polymerization. Authors: Henry C Nguyen / Nathaniel Talledge / John McCullough / Abhimanyu Sharma / Frank R Moss / Janet H Iwasa / Michael D Vershinin / Wesley I Sundquist / Adam Frost / Abstract: The 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.
Entire : Helical copolymer of CHMP1B and IST1 bound to a lipid membrane na...
Entire
Name: Helical copolymer of CHMP1B and IST1 bound to a lipid membrane nanotube
Components
Complex: Helical copolymer of CHMP1B and IST1 bound to a lipid membrane nanotube
Protein or peptide: CHMP1B
Protein or peptide: IST1
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Supramolecule #1: Helical copolymer of CHMP1B and IST1 bound to a lipid membrane na...
Supramolecule
Name: Helical copolymer of CHMP1B and IST1 bound to a lipid membrane nanotube type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: The lipid nanotube contains an iodinated analog of cholesterol
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