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Title: Structure and membrane remodeling activity of ESCRT-III helical polymers

Abstract

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.

Authors:
; ; ; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
National Institutes of Health (NIH); National Science Foundation (NSF); USDOE Office of Science (SC)
OSTI Identifier:
1355856
Alternate Identifier(s):
OSTI ID: 1257996; OSTI ID: 1378702
Grant/Contract Number:  
AC02-05CH11231; DGE-1143954; 2P50GM082545-06; R01GM112080; R01AI051174; 1DP2GM110772-01; 1P01 GM063210; R01GM076686; R01NS050717
Resource Type:
Published Article
Journal Name:
Science
Additional Journal Information:
Journal Name: Science Journal Volume: 350 Journal Issue: 6267; Journal ID: ISSN 0036-8075
Publisher:
American Association for the Advancement of Science (AAAS)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES

Citation Formats

McCullough, J., Clippinger, A. K., Talledge, N., Skowyra, M. L., Saunders, M. G., Naismith, T. V., Colf, L. A., Afonine, P., Arthur, C., Sundquist, W. I., Hanson, P. I., and Frost, A. Structure and membrane remodeling activity of ESCRT-III helical polymers. United States: N. p., 2015. Web. doi:10.1126/science.aad8305.
McCullough, J., Clippinger, A. K., Talledge, N., Skowyra, M. L., Saunders, M. G., Naismith, T. V., Colf, L. A., Afonine, P., Arthur, C., Sundquist, W. I., Hanson, P. I., & Frost, A. Structure and membrane remodeling activity of ESCRT-III helical polymers. United States. https://doi.org/10.1126/science.aad8305
McCullough, J., Clippinger, A. K., Talledge, N., Skowyra, M. L., Saunders, M. G., Naismith, T. V., Colf, L. A., Afonine, P., Arthur, C., Sundquist, W. I., Hanson, P. I., and Frost, A. Thu . "Structure and membrane remodeling activity of ESCRT-III helical polymers". United States. https://doi.org/10.1126/science.aad8305.
@article{osti_1355856,
title = {Structure and membrane remodeling activity of ESCRT-III helical polymers},
author = {McCullough, J. and Clippinger, A. K. and Talledge, N. and Skowyra, M. L. and Saunders, M. G. and Naismith, T. V. and Colf, L. A. and Afonine, P. and Arthur, C. and Sundquist, W. I. and Hanson, P. I. and Frost, A.},
abstractNote = {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.},
doi = {10.1126/science.aad8305},
journal = {Science},
number = 6267,
volume = 350,
place = {United States},
year = {Thu Dec 03 00:00:00 EST 2015},
month = {Thu Dec 03 00:00:00 EST 2015}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.1126/science.aad8305

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