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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. In conclusion, our analysis suggests how common ESCRT-III filament architectures could stabilize different degrees and directions of membrane curvature.

Authors:
 [1];  [2];  [3];  [2];  [1];  [2];  [1];  [4];  [5];  [1];  [2];  [3]
  1. Univ. of Utah, Salt Lake City, UT (United States)
  2. Washington Univ. School of Medicine, St. Louis, MO (United States)
  3. Univ. of Utah, Salt Lake City, UT (United States); Univ. of California, San Francisco, CA (United States)
  4. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
  5. FEI Company, Hillsboro, OR (United States)
Publication Date:
Research Org.:
Lawrence Berkeley National Lab. (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 Volume: 350; Journal Issue: 6267; Journal ID: ISSN 0036-8075
Publisher:
AAAS
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES

Citation Formats

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., and Frost, Adam. Structure and membrane remodeling activity of ESCRT-III helical polymers. United States: N. p., 2015. Web. doi:10.1126/science.aad8305.
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. Structure and membrane remodeling activity of ESCRT-III helical polymers. United States. doi:10.1126/science.aad8305.
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., and Frost, Adam. Fri . "Structure and membrane remodeling activity of ESCRT-III helical polymers". United States. doi:10.1126/science.aad8305.
@article{osti_1355856,
title = {Structure and membrane remodeling activity of ESCRT-III helical polymers},
author = {McCullough, John and Clippinger, Amy K. and Talledge, Nathaniel and Skowyra, Michael L. and Saunders, Marissa G. and Naismith, Teresa V. and Colf, Leremy A. and Afonine, Pavel and Arthur, Christopher and Sundquist, Wesley I. and Hanson, Phyllis I. and Frost, Adam},
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. In conclusion, 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 = {2015},
month = {12}
}

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

Citation Metrics:
Cited by: 33 works
Citation information provided by
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