Molecular mechanism for direct actin force-sensing by α-catenin

The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulate...
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Autor*in:	Lin Mei [verfasserIn] Santiago Espinosa de los Reyes [verfasserIn] Matthew J Reynolds [verfasserIn] Rachel Leicher [verfasserIn] Shixin Liu [verfasserIn] Gregory M Alushin [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	cryo-electron microscopy actin cytoskeleton mechanobiology mechanosensation cell adhesion single molecule biophysics

Übergeordnetes Werk:	In: eLife - eLife Sciences Publications Ltd, 2013, 9(2020)
Übergeordnetes Werk:	volume:9 ; year:2020

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.7554/eLife.62514

Katalog-ID:	DOAJ084122013

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520			\|a The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulated. Here we employ both optical trapping and biochemical reconstitution with myosin motor proteins to show single piconewton forces applied solely to F-actin enhance binding by the human version of the essential cell-cell adhesion protein αE-catenin but not its homolog vinculin. Cryo-electron microscopy structures of both proteins bound to F-actin reveal unique rearrangements that facilitate their flexible C-termini refolding to engage distinct interfaces. Truncating α-catenin’s C-terminus eliminates force-activated F-actin binding, and addition of this motif to vinculin confers force-activated binding, demonstrating that α-catenin’s C-terminus is a modular detector of F-actin tension. Our studies establish that piconewton force on F-actin can enhance partner binding, which we propose mechanically regulates cellular adhesion through α-catenin.
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allfields	10.7554/eLife.62514 doi (DE-627)DOAJ084122013 (DE-599)DOAJb10232867b744f808e382a22565469d5 DE-627 ger DE-627 rakwb eng QH301-705.5 Lin Mei verfasserin aut Molecular mechanism for direct actin force-sensing by α-catenin 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulated. Here we employ both optical trapping and biochemical reconstitution with myosin motor proteins to show single piconewton forces applied solely to F-actin enhance binding by the human version of the essential cell-cell adhesion protein αE-catenin but not its homolog vinculin. Cryo-electron microscopy structures of both proteins bound to F-actin reveal unique rearrangements that facilitate their flexible C-termini refolding to engage distinct interfaces. Truncating α-catenin’s C-terminus eliminates force-activated F-actin binding, and addition of this motif to vinculin confers force-activated binding, demonstrating that α-catenin’s C-terminus is a modular detector of F-actin tension. Our studies establish that piconewton force on F-actin can enhance partner binding, which we propose mechanically regulates cellular adhesion through α-catenin. cryo-electron microscopy actin cytoskeleton mechanobiology mechanosensation cell adhesion single molecule biophysics Medicine R Science Q Biology (General) Santiago Espinosa de los Reyes verfasserin aut Matthew J Reynolds verfasserin aut Rachel Leicher verfasserin aut Shixin Liu verfasserin aut Gregory M Alushin verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.62514 kostenfrei https://doaj.org/article/b10232867b744f808e382a22565469d5 kostenfrei https://elifesciences.org/articles/62514 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
spelling	10.7554/eLife.62514 doi (DE-627)DOAJ084122013 (DE-599)DOAJb10232867b744f808e382a22565469d5 DE-627 ger DE-627 rakwb eng QH301-705.5 Lin Mei verfasserin aut Molecular mechanism for direct actin force-sensing by α-catenin 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulated. Here we employ both optical trapping and biochemical reconstitution with myosin motor proteins to show single piconewton forces applied solely to F-actin enhance binding by the human version of the essential cell-cell adhesion protein αE-catenin but not its homolog vinculin. Cryo-electron microscopy structures of both proteins bound to F-actin reveal unique rearrangements that facilitate their flexible C-termini refolding to engage distinct interfaces. Truncating α-catenin’s C-terminus eliminates force-activated F-actin binding, and addition of this motif to vinculin confers force-activated binding, demonstrating that α-catenin’s C-terminus is a modular detector of F-actin tension. Our studies establish that piconewton force on F-actin can enhance partner binding, which we propose mechanically regulates cellular adhesion through α-catenin. cryo-electron microscopy actin cytoskeleton mechanobiology mechanosensation cell adhesion single molecule biophysics Medicine R Science Q Biology (General) Santiago Espinosa de los Reyes verfasserin aut Matthew J Reynolds verfasserin aut Rachel Leicher verfasserin aut Shixin Liu verfasserin aut Gregory M Alushin verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.62514 kostenfrei https://doaj.org/article/b10232867b744f808e382a22565469d5 kostenfrei https://elifesciences.org/articles/62514 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
allfields_unstemmed	10.7554/eLife.62514 doi (DE-627)DOAJ084122013 (DE-599)DOAJb10232867b744f808e382a22565469d5 DE-627 ger DE-627 rakwb eng QH301-705.5 Lin Mei verfasserin aut Molecular mechanism for direct actin force-sensing by α-catenin 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulated. Here we employ both optical trapping and biochemical reconstitution with myosin motor proteins to show single piconewton forces applied solely to F-actin enhance binding by the human version of the essential cell-cell adhesion protein αE-catenin but not its homolog vinculin. Cryo-electron microscopy structures of both proteins bound to F-actin reveal unique rearrangements that facilitate their flexible C-termini refolding to engage distinct interfaces. Truncating α-catenin’s C-terminus eliminates force-activated F-actin binding, and addition of this motif to vinculin confers force-activated binding, demonstrating that α-catenin’s C-terminus is a modular detector of F-actin tension. Our studies establish that piconewton force on F-actin can enhance partner binding, which we propose mechanically regulates cellular adhesion through α-catenin. cryo-electron microscopy actin cytoskeleton mechanobiology mechanosensation cell adhesion single molecule biophysics Medicine R Science Q Biology (General) Santiago Espinosa de los Reyes verfasserin aut Matthew J Reynolds verfasserin aut Rachel Leicher verfasserin aut Shixin Liu verfasserin aut Gregory M Alushin verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.62514 kostenfrei https://doaj.org/article/b10232867b744f808e382a22565469d5 kostenfrei https://elifesciences.org/articles/62514 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
allfieldsGer	10.7554/eLife.62514 doi (DE-627)DOAJ084122013 (DE-599)DOAJb10232867b744f808e382a22565469d5 DE-627 ger DE-627 rakwb eng QH301-705.5 Lin Mei verfasserin aut Molecular mechanism for direct actin force-sensing by α-catenin 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulated. Here we employ both optical trapping and biochemical reconstitution with myosin motor proteins to show single piconewton forces applied solely to F-actin enhance binding by the human version of the essential cell-cell adhesion protein αE-catenin but not its homolog vinculin. Cryo-electron microscopy structures of both proteins bound to F-actin reveal unique rearrangements that facilitate their flexible C-termini refolding to engage distinct interfaces. Truncating α-catenin’s C-terminus eliminates force-activated F-actin binding, and addition of this motif to vinculin confers force-activated binding, demonstrating that α-catenin’s C-terminus is a modular detector of F-actin tension. Our studies establish that piconewton force on F-actin can enhance partner binding, which we propose mechanically regulates cellular adhesion through α-catenin. cryo-electron microscopy actin cytoskeleton mechanobiology mechanosensation cell adhesion single molecule biophysics Medicine R Science Q Biology (General) Santiago Espinosa de los Reyes verfasserin aut Matthew J Reynolds verfasserin aut Rachel Leicher verfasserin aut Shixin Liu verfasserin aut Gregory M Alushin verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.62514 kostenfrei https://doaj.org/article/b10232867b744f808e382a22565469d5 kostenfrei https://elifesciences.org/articles/62514 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
allfieldsSound	10.7554/eLife.62514 doi (DE-627)DOAJ084122013 (DE-599)DOAJb10232867b744f808e382a22565469d5 DE-627 ger DE-627 rakwb eng QH301-705.5 Lin Mei verfasserin aut Molecular mechanism for direct actin force-sensing by α-catenin 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulated. Here we employ both optical trapping and biochemical reconstitution with myosin motor proteins to show single piconewton forces applied solely to F-actin enhance binding by the human version of the essential cell-cell adhesion protein αE-catenin but not its homolog vinculin. Cryo-electron microscopy structures of both proteins bound to F-actin reveal unique rearrangements that facilitate their flexible C-termini refolding to engage distinct interfaces. Truncating α-catenin’s C-terminus eliminates force-activated F-actin binding, and addition of this motif to vinculin confers force-activated binding, demonstrating that α-catenin’s C-terminus is a modular detector of F-actin tension. Our studies establish that piconewton force on F-actin can enhance partner binding, which we propose mechanically regulates cellular adhesion through α-catenin. cryo-electron microscopy actin cytoskeleton mechanobiology mechanosensation cell adhesion single molecule biophysics Medicine R Science Q Biology (General) Santiago Espinosa de los Reyes verfasserin aut Matthew J Reynolds verfasserin aut Rachel Leicher verfasserin aut Shixin Liu verfasserin aut Gregory M Alushin verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 9(2020) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:9 year:2020 https://doi.org/10.7554/eLife.62514 kostenfrei https://doaj.org/article/b10232867b744f808e382a22565469d5 kostenfrei https://elifesciences.org/articles/62514 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2020
language	English
source	In eLife 9(2020) volume:9 year:2020
sourceStr	In eLife 9(2020) volume:9 year:2020
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container_title	eLife
authorswithroles_txt_mv	Lin Mei @@aut@@ Santiago Espinosa de los Reyes @@aut@@ Matthew J Reynolds @@aut@@ Rachel Leicher @@aut@@ Shixin Liu @@aut@@ Gregory M Alushin @@aut@@
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author	Lin Mei
spellingShingle	Lin Mei misc QH301-705.5 misc cryo-electron microscopy misc actin cytoskeleton misc mechanobiology misc mechanosensation misc cell adhesion misc single molecule biophysics misc Medicine misc R misc Science misc Q misc Biology (General) Molecular mechanism for direct actin force-sensing by α-catenin
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topic_title	QH301-705.5 Molecular mechanism for direct actin force-sensing by α-catenin cryo-electron microscopy actin cytoskeleton mechanobiology mechanosensation cell adhesion single molecule biophysics
topic	misc QH301-705.5 misc cryo-electron microscopy misc actin cytoskeleton misc mechanobiology misc mechanosensation misc cell adhesion misc single molecule biophysics misc Medicine misc R misc Science misc Q misc Biology (General)
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title	Molecular mechanism for direct actin force-sensing by α-catenin
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title_full	Molecular mechanism for direct actin force-sensing by α-catenin
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title_sort	molecular mechanism for direct actin force-sensing by α-catenin
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title_auth	Molecular mechanism for direct actin force-sensing by α-catenin
abstract	The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulated. Here we employ both optical trapping and biochemical reconstitution with myosin motor proteins to show single piconewton forces applied solely to F-actin enhance binding by the human version of the essential cell-cell adhesion protein αE-catenin but not its homolog vinculin. Cryo-electron microscopy structures of both proteins bound to F-actin reveal unique rearrangements that facilitate their flexible C-termini refolding to engage distinct interfaces. Truncating α-catenin’s C-terminus eliminates force-activated F-actin binding, and addition of this motif to vinculin confers force-activated binding, demonstrating that α-catenin’s C-terminus is a modular detector of F-actin tension. Our studies establish that piconewton force on F-actin can enhance partner binding, which we propose mechanically regulates cellular adhesion through α-catenin.
abstractGer	The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulated. Here we employ both optical trapping and biochemical reconstitution with myosin motor proteins to show single piconewton forces applied solely to F-actin enhance binding by the human version of the essential cell-cell adhesion protein αE-catenin but not its homolog vinculin. Cryo-electron microscopy structures of both proteins bound to F-actin reveal unique rearrangements that facilitate their flexible C-termini refolding to engage distinct interfaces. Truncating α-catenin’s C-terminus eliminates force-activated F-actin binding, and addition of this motif to vinculin confers force-activated binding, demonstrating that α-catenin’s C-terminus is a modular detector of F-actin tension. Our studies establish that piconewton force on F-actin can enhance partner binding, which we propose mechanically regulates cellular adhesion through α-catenin.
abstract_unstemmed	The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulated. Here we employ both optical trapping and biochemical reconstitution with myosin motor proteins to show single piconewton forces applied solely to F-actin enhance binding by the human version of the essential cell-cell adhesion protein αE-catenin but not its homolog vinculin. Cryo-electron microscopy structures of both proteins bound to F-actin reveal unique rearrangements that facilitate their flexible C-termini refolding to engage distinct interfaces. Truncating α-catenin’s C-terminus eliminates force-activated F-actin binding, and addition of this motif to vinculin confers force-activated binding, demonstrating that α-catenin’s C-terminus is a modular detector of F-actin tension. Our studies establish that piconewton force on F-actin can enhance partner binding, which we propose mechanically regulates cellular adhesion through α-catenin.
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title_short	Molecular mechanism for direct actin force-sensing by α-catenin
url	https://doi.org/10.7554/eLife.62514 https://doaj.org/article/b10232867b744f808e382a22565469d5 https://elifesciences.org/articles/62514 https://doaj.org/toc/2050-084X
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