Angiomotin functions in HIV-1 assembly and budding

Many retroviral Gag proteins contain PPXY late assembly domain motifs that recruit proteins of the NEDD4 E3 ubiquitin ligase family to facilitate virus release. Overexpression of NEDD4L can also stimulate HIV-1 release but in this case the Gag protein lacks a PPXY motif, suggesting that NEDD4L may f...
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Autor*in:	Gaelle Mercenne [verfasserIn] Steven L Alam [verfasserIn] Jun Arii [verfasserIn] Matthew S Lalonde [verfasserIn] Wesley I Sundquist [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2015

Schlagwörter:	HIV Gag protein NEDD4L motin protein family ESCRT pathway virus-host interaction

Übergeordnetes Werk:	In: eLife - eLife Sciences Publications Ltd, 2013, 4(2015)
Übergeordnetes Werk:	volume:4 ; year:2015

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.7554/eLife.03778

Katalog-ID:	DOAJ021057699

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520			\|a Many retroviral Gag proteins contain PPXY late assembly domain motifs that recruit proteins of the NEDD4 E3 ubiquitin ligase family to facilitate virus release. Overexpression of NEDD4L can also stimulate HIV-1 release but in this case the Gag protein lacks a PPXY motif, suggesting that NEDD4L may function through an adaptor protein. Here, we demonstrate that the cellular protein Angiomotin (AMOT) can bind both NEDD4L and HIV-1 Gag. HIV-1 release and infectivity are stimulated by AMOT overexpression and inhibited by AMOT depletion, whereas AMOT mutants that cannot bind NEDD4L cannot function in virus release. Electron microscopic analyses revealed that in the absence of AMOT assembling Gag molecules fail to form a fully spherical enveloped particle. Our experiments indicate that AMOT and other motin family members function together with NEDD4L to help complete immature virion assembly prior to ESCRT-mediated virus budding.
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Indexfelder

author_variant	g m gm s l a sla j a ja m s l msl w i s wis
matchkey_str	article:2050084X:2015----::nimtnucinihvasm
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allfields	10.7554/eLife.03778 doi (DE-627)DOAJ021057699 (DE-599)DOAJ983ae360e41f45409ecc2ed7090babbb DE-627 ger DE-627 rakwb eng QH301-705.5 Gaelle Mercenne verfasserin aut Angiomotin functions in HIV-1 assembly and budding 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Many retroviral Gag proteins contain PPXY late assembly domain motifs that recruit proteins of the NEDD4 E3 ubiquitin ligase family to facilitate virus release. Overexpression of NEDD4L can also stimulate HIV-1 release but in this case the Gag protein lacks a PPXY motif, suggesting that NEDD4L may function through an adaptor protein. Here, we demonstrate that the cellular protein Angiomotin (AMOT) can bind both NEDD4L and HIV-1 Gag. HIV-1 release and infectivity are stimulated by AMOT overexpression and inhibited by AMOT depletion, whereas AMOT mutants that cannot bind NEDD4L cannot function in virus release. Electron microscopic analyses revealed that in the absence of AMOT assembling Gag molecules fail to form a fully spherical enveloped particle. Our experiments indicate that AMOT and other motin family members function together with NEDD4L to help complete immature virion assembly prior to ESCRT-mediated virus budding. HIV Gag protein NEDD4L motin protein family ESCRT pathway virus-host interaction Medicine R Science Q Biology (General) Steven L Alam verfasserin aut Jun Arii verfasserin aut Matthew S Lalonde verfasserin aut Wesley I Sundquist verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 4(2015) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:4 year:2015 https://doi.org/10.7554/eLife.03778 kostenfrei https://doaj.org/article/983ae360e41f45409ecc2ed7090babbb kostenfrei https://elifesciences.org/articles/03778 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 4 2015
spelling	10.7554/eLife.03778 doi (DE-627)DOAJ021057699 (DE-599)DOAJ983ae360e41f45409ecc2ed7090babbb DE-627 ger DE-627 rakwb eng QH301-705.5 Gaelle Mercenne verfasserin aut Angiomotin functions in HIV-1 assembly and budding 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Many retroviral Gag proteins contain PPXY late assembly domain motifs that recruit proteins of the NEDD4 E3 ubiquitin ligase family to facilitate virus release. Overexpression of NEDD4L can also stimulate HIV-1 release but in this case the Gag protein lacks a PPXY motif, suggesting that NEDD4L may function through an adaptor protein. Here, we demonstrate that the cellular protein Angiomotin (AMOT) can bind both NEDD4L and HIV-1 Gag. HIV-1 release and infectivity are stimulated by AMOT overexpression and inhibited by AMOT depletion, whereas AMOT mutants that cannot bind NEDD4L cannot function in virus release. Electron microscopic analyses revealed that in the absence of AMOT assembling Gag molecules fail to form a fully spherical enveloped particle. Our experiments indicate that AMOT and other motin family members function together with NEDD4L to help complete immature virion assembly prior to ESCRT-mediated virus budding. HIV Gag protein NEDD4L motin protein family ESCRT pathway virus-host interaction Medicine R Science Q Biology (General) Steven L Alam verfasserin aut Jun Arii verfasserin aut Matthew S Lalonde verfasserin aut Wesley I Sundquist verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 4(2015) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:4 year:2015 https://doi.org/10.7554/eLife.03778 kostenfrei https://doaj.org/article/983ae360e41f45409ecc2ed7090babbb kostenfrei https://elifesciences.org/articles/03778 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 4 2015
allfields_unstemmed	10.7554/eLife.03778 doi (DE-627)DOAJ021057699 (DE-599)DOAJ983ae360e41f45409ecc2ed7090babbb DE-627 ger DE-627 rakwb eng QH301-705.5 Gaelle Mercenne verfasserin aut Angiomotin functions in HIV-1 assembly and budding 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Many retroviral Gag proteins contain PPXY late assembly domain motifs that recruit proteins of the NEDD4 E3 ubiquitin ligase family to facilitate virus release. Overexpression of NEDD4L can also stimulate HIV-1 release but in this case the Gag protein lacks a PPXY motif, suggesting that NEDD4L may function through an adaptor protein. Here, we demonstrate that the cellular protein Angiomotin (AMOT) can bind both NEDD4L and HIV-1 Gag. HIV-1 release and infectivity are stimulated by AMOT overexpression and inhibited by AMOT depletion, whereas AMOT mutants that cannot bind NEDD4L cannot function in virus release. Electron microscopic analyses revealed that in the absence of AMOT assembling Gag molecules fail to form a fully spherical enveloped particle. Our experiments indicate that AMOT and other motin family members function together with NEDD4L to help complete immature virion assembly prior to ESCRT-mediated virus budding. HIV Gag protein NEDD4L motin protein family ESCRT pathway virus-host interaction Medicine R Science Q Biology (General) Steven L Alam verfasserin aut Jun Arii verfasserin aut Matthew S Lalonde verfasserin aut Wesley I Sundquist verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 4(2015) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:4 year:2015 https://doi.org/10.7554/eLife.03778 kostenfrei https://doaj.org/article/983ae360e41f45409ecc2ed7090babbb kostenfrei https://elifesciences.org/articles/03778 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 4 2015
allfieldsGer	10.7554/eLife.03778 doi (DE-627)DOAJ021057699 (DE-599)DOAJ983ae360e41f45409ecc2ed7090babbb DE-627 ger DE-627 rakwb eng QH301-705.5 Gaelle Mercenne verfasserin aut Angiomotin functions in HIV-1 assembly and budding 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Many retroviral Gag proteins contain PPXY late assembly domain motifs that recruit proteins of the NEDD4 E3 ubiquitin ligase family to facilitate virus release. Overexpression of NEDD4L can also stimulate HIV-1 release but in this case the Gag protein lacks a PPXY motif, suggesting that NEDD4L may function through an adaptor protein. Here, we demonstrate that the cellular protein Angiomotin (AMOT) can bind both NEDD4L and HIV-1 Gag. HIV-1 release and infectivity are stimulated by AMOT overexpression and inhibited by AMOT depletion, whereas AMOT mutants that cannot bind NEDD4L cannot function in virus release. Electron microscopic analyses revealed that in the absence of AMOT assembling Gag molecules fail to form a fully spherical enveloped particle. Our experiments indicate that AMOT and other motin family members function together with NEDD4L to help complete immature virion assembly prior to ESCRT-mediated virus budding. HIV Gag protein NEDD4L motin protein family ESCRT pathway virus-host interaction Medicine R Science Q Biology (General) Steven L Alam verfasserin aut Jun Arii verfasserin aut Matthew S Lalonde verfasserin aut Wesley I Sundquist verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 4(2015) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:4 year:2015 https://doi.org/10.7554/eLife.03778 kostenfrei https://doaj.org/article/983ae360e41f45409ecc2ed7090babbb kostenfrei https://elifesciences.org/articles/03778 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 4 2015
allfieldsSound	10.7554/eLife.03778 doi (DE-627)DOAJ021057699 (DE-599)DOAJ983ae360e41f45409ecc2ed7090babbb DE-627 ger DE-627 rakwb eng QH301-705.5 Gaelle Mercenne verfasserin aut Angiomotin functions in HIV-1 assembly and budding 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Many retroviral Gag proteins contain PPXY late assembly domain motifs that recruit proteins of the NEDD4 E3 ubiquitin ligase family to facilitate virus release. Overexpression of NEDD4L can also stimulate HIV-1 release but in this case the Gag protein lacks a PPXY motif, suggesting that NEDD4L may function through an adaptor protein. Here, we demonstrate that the cellular protein Angiomotin (AMOT) can bind both NEDD4L and HIV-1 Gag. HIV-1 release and infectivity are stimulated by AMOT overexpression and inhibited by AMOT depletion, whereas AMOT mutants that cannot bind NEDD4L cannot function in virus release. Electron microscopic analyses revealed that in the absence of AMOT assembling Gag molecules fail to form a fully spherical enveloped particle. Our experiments indicate that AMOT and other motin family members function together with NEDD4L to help complete immature virion assembly prior to ESCRT-mediated virus budding. HIV Gag protein NEDD4L motin protein family ESCRT pathway virus-host interaction Medicine R Science Q Biology (General) Steven L Alam verfasserin aut Jun Arii verfasserin aut Matthew S Lalonde verfasserin aut Wesley I Sundquist verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 4(2015) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:4 year:2015 https://doi.org/10.7554/eLife.03778 kostenfrei https://doaj.org/article/983ae360e41f45409ecc2ed7090babbb kostenfrei https://elifesciences.org/articles/03778 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 4 2015
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authorswithroles_txt_mv	Gaelle Mercenne @@aut@@ Steven L Alam @@aut@@ Jun Arii @@aut@@ Matthew S Lalonde @@aut@@ Wesley I Sundquist @@aut@@
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callnumber-first	Q - Science
author	Gaelle Mercenne
spellingShingle	Gaelle Mercenne misc QH301-705.5 misc HIV Gag protein misc NEDD4L misc motin protein family misc ESCRT pathway misc virus-host interaction misc Medicine misc R misc Science misc Q misc Biology (General) Angiomotin functions in HIV-1 assembly and budding
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topic_title	QH301-705.5 Angiomotin functions in HIV-1 assembly and budding HIV Gag protein NEDD4L motin protein family ESCRT pathway virus-host interaction
topic	misc QH301-705.5 misc HIV Gag protein misc NEDD4L misc motin protein family misc ESCRT pathway misc virus-host interaction misc Medicine misc R misc Science misc Q misc Biology (General)
topic_unstemmed	misc QH301-705.5 misc HIV Gag protein misc NEDD4L misc motin protein family misc ESCRT pathway misc virus-host interaction misc Medicine misc R misc Science misc Q misc Biology (General)
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title	Angiomotin functions in HIV-1 assembly and budding
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title_full	Angiomotin functions in HIV-1 assembly and budding
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author_browse	Gaelle Mercenne Steven L Alam Jun Arii Matthew S Lalonde Wesley I Sundquist
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title_sort	angiomotin functions in hiv-1 assembly and budding
callnumber	QH301-705.5
title_auth	Angiomotin functions in HIV-1 assembly and budding
abstract	Many retroviral Gag proteins contain PPXY late assembly domain motifs that recruit proteins of the NEDD4 E3 ubiquitin ligase family to facilitate virus release. Overexpression of NEDD4L can also stimulate HIV-1 release but in this case the Gag protein lacks a PPXY motif, suggesting that NEDD4L may function through an adaptor protein. Here, we demonstrate that the cellular protein Angiomotin (AMOT) can bind both NEDD4L and HIV-1 Gag. HIV-1 release and infectivity are stimulated by AMOT overexpression and inhibited by AMOT depletion, whereas AMOT mutants that cannot bind NEDD4L cannot function in virus release. Electron microscopic analyses revealed that in the absence of AMOT assembling Gag molecules fail to form a fully spherical enveloped particle. Our experiments indicate that AMOT and other motin family members function together with NEDD4L to help complete immature virion assembly prior to ESCRT-mediated virus budding.
abstractGer	Many retroviral Gag proteins contain PPXY late assembly domain motifs that recruit proteins of the NEDD4 E3 ubiquitin ligase family to facilitate virus release. Overexpression of NEDD4L can also stimulate HIV-1 release but in this case the Gag protein lacks a PPXY motif, suggesting that NEDD4L may function through an adaptor protein. Here, we demonstrate that the cellular protein Angiomotin (AMOT) can bind both NEDD4L and HIV-1 Gag. HIV-1 release and infectivity are stimulated by AMOT overexpression and inhibited by AMOT depletion, whereas AMOT mutants that cannot bind NEDD4L cannot function in virus release. Electron microscopic analyses revealed that in the absence of AMOT assembling Gag molecules fail to form a fully spherical enveloped particle. Our experiments indicate that AMOT and other motin family members function together with NEDD4L to help complete immature virion assembly prior to ESCRT-mediated virus budding.
abstract_unstemmed	Many retroviral Gag proteins contain PPXY late assembly domain motifs that recruit proteins of the NEDD4 E3 ubiquitin ligase family to facilitate virus release. Overexpression of NEDD4L can also stimulate HIV-1 release but in this case the Gag protein lacks a PPXY motif, suggesting that NEDD4L may function through an adaptor protein. Here, we demonstrate that the cellular protein Angiomotin (AMOT) can bind both NEDD4L and HIV-1 Gag. HIV-1 release and infectivity are stimulated by AMOT overexpression and inhibited by AMOT depletion, whereas AMOT mutants that cannot bind NEDD4L cannot function in virus release. Electron microscopic analyses revealed that in the absence of AMOT assembling Gag molecules fail to form a fully spherical enveloped particle. Our experiments indicate that AMOT and other motin family members function together with NEDD4L to help complete immature virion assembly prior to ESCRT-mediated virus budding.
collection_details	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
title_short	Angiomotin functions in HIV-1 assembly and budding
url	https://doi.org/10.7554/eLife.03778 https://doaj.org/article/983ae360e41f45409ecc2ed7090babbb https://elifesciences.org/articles/03778 https://doaj.org/toc/2050-084X
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author2	Steven L Alam Jun Arii Matthew S Lalonde Wesley I Sundquist
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up_date	2024-07-03T18:38:01.624Z
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