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Structure and membrane remodeling activity of ESCRT-III helical polymers.

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Title: Structure and membrane remodeling activity of ESCRT-III helical polymers.
Authors: 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
Source: Science (pre-March 2025). 12/18/2015, Vol. 350 Issue 6267, p1548-1551. 4p.
Subjects: Protein analysis, Copolymers, Electron microscopy, Polymer analysis, Sodium
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. [ABSTRACT FROM AUTHOR]
Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: Structure and membrane remodeling activity of ESCRT-III helical polymers.
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  Data: <searchLink fieldCode="AR" term="%22McCullough%2C+John%22">McCullough, John</searchLink><br /><searchLink fieldCode="AR" term="%22Clippinger%2C+Amy+K%2E%22">Clippinger, Amy K.</searchLink><br /><searchLink fieldCode="AR" term="%22Talledge%2C+Nathaniel%22">Talledge, Nathaniel</searchLink><br /><searchLink fieldCode="AR" term="%22Skowyra%2C+Michael+L%2E%22">Skowyra, Michael L.</searchLink><br /><searchLink fieldCode="AR" term="%22Saunders%2C+Marissa+G%2E%22">Saunders, Marissa G.</searchLink><br /><searchLink fieldCode="AR" term="%22Naismith%2C+Teresa+V%2E%22">Naismith, Teresa V.</searchLink><br /><searchLink fieldCode="AR" term="%22Colf%2C+Leremy+A%2E%22">Colf, Leremy A.</searchLink><br /><searchLink fieldCode="AR" term="%22Afonine%2C+Pavel%22">Afonine, Pavel</searchLink><br /><searchLink fieldCode="AR" term="%22Arthur%2C+Christopher%22">Arthur, Christopher</searchLink><br /><searchLink fieldCode="AR" term="%22Sundquist%2C+Wesley+I%2E%22">Sundquist, Wesley I.</searchLink><br /><searchLink fieldCode="AR" term="%22Hanson%2C+Phyllis+I%2E%22">Hanson, Phyllis I.</searchLink><br /><searchLink fieldCode="AR" term="%22Frost%2C+Adam%22">Frost, Adam</searchLink>
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  Data: <searchLink fieldCode="JN" term="%22Science+%28pre-March+2025%29%22">Science (pre-March 2025)</searchLink>. 12/18/2015, Vol. 350 Issue 6267, p1548-1551. 4p.
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  Data: <searchLink fieldCode="DE" term="%22Protein+analysis%22">Protein analysis</searchLink><br /><searchLink fieldCode="DE" term="%22Copolymers%22">Copolymers</searchLink><br /><searchLink fieldCode="DE" term="%22Electron+microscopy%22">Electron microscopy</searchLink><br /><searchLink fieldCode="DE" term="%22Polymer+analysis%22">Polymer analysis</searchLink><br /><searchLink fieldCode="DE" term="%22Sodium%22">Sodium</searchLink>
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  Data: 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. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=pbh&AN=111875205
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              Text: 12/18/2015
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