Structure and membrane remodeling activity of ESCRT-III helical polymers

McCullough, John; Clippinger, Amy K.; Talledge, Nathaniel; Skowyra, Michael L.; Saunders, Marissa G.; Naismith, Teresa V.; Colf, Leremy A.; Afonine, Pavel; Arthur, Christopher; Sundquist, Wesley I.; Hanson, Phyllis I.; Frost, Adam

doi:10.1126/science.aad8305

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Structure and membrane remodeling activity of ESCRT-III helical polymers

Published Date:

Dec 03 2015

Publisher's site:

http://dx.doi.org/10.1126/science.aad8305 New Site Icon

Source:

Science. 350(6267):1548-1551.

[PDF-2.03 MB]

Details:

Alternative Title:

Science

Personal Author:

McCullough, John ; Clippinger, Amy K. ; Talledge, Nathaniel ; Skowyra, Michael L. ; Saunders, Marissa G. ; ... More ▼

Description:

The endosomal sorting complexes required for transport (ESCRT) proteins mediate fundamental membrane remodeling events that require stabilizing negative membrane curvature. These include endosomal intralumenal vesicle formation, HIV budding, nuclear envelope closure, and cytokinetic abscission. ESCRT-III subunits perform key roles in these processes by changing conformation and polymerizing into membrane-remodeling filaments. Here, we report the 4 angstrom resolution cryogenic electron microscopy reconstruction of a one-start, double-stranded helical copolymer composed of two different human ESCRT-III subunits, charged multivesicular body protein 1B (CHMP1B) and increased sodium tolerance 1 (IST1). The inner strand comprises "open" CHMP1B subunits that interlock in an elaborate domain-swapped architecture and is encircled by an outer strand of "closed" IST1 subunits. Unlike other ESCRT-III proteins, CHMP1B and IST1 polymers form external coats on positively curved membranes in vitro and in vivo. Our analysis suggests how common ESCRT-III filament architectures could stabilize different degrees and directions of membrane curvature.

Subject:

[+]

Pubmed ID:

26634441

Pubmed Central ID:

PMC4684769

Document Type:

Journal Article

Funding:

1DP2GM110772-01/DP/NCCDPHP CDC HHS/United States ; 1P01 GM063210/GM/NIGMS NIH HHS/United States ; 2P50GM082545-06/GM/NIGMS NIH HHS/United States ; DP2 GM110772/GM/NIGMS NIH HHS/United States ; P01 GM063210/GM/NIGMS NIH HHS/United States ; ... More ▼

Collection(s):

CDC Public Access

Main Document Checksum:

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Supporting Files:

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