Mammalian Staufen 1 is recruited to stress granules and impairs their assembly

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Stress granules are cytoplasmic mRNA-silencing foci that form transiently during the stress response. Stress granules harbor abortive translation initiation complexes and are in dynamic equilibrium with translating polysomes. Mammalian Staufen 1 (Stau1) is a ubiquitous double-stranded RNA-binding pr...

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Autores principales:	Thomas, M.G., Martinez Tosar, L.J., Desbats, M.A., Leishman, C.C., Boccaccio, G.L.
Formato:	Artículo publishedVersion
Lenguaje:	Inglés
Publicado:	2009
Materias:	ER stress Oxidative stress P bodies Silencing foci Staufen Stress granules initiation factor 2alpha RNA binding protein staufen 1 unclassified drug enzyme inhibitor heat shock protein 70 initiation factor 2 small interfering RNA staufen protein, mammalian thapsigargin animal cell article cell granule cellular stress response controlled study endoplasmic reticulum stress gene overexpression gene silencing human human cell nonhuman oxidative stress polysome priority journal protein assembly protein phosphorylation regulatory mechanism translation initiation animal biosynthesis cell strain 3T3 cell strain COS1 Cercopithecus chemistry confocal microscopy drug effect endoplasmic reticulum HeLa cell metabolism mouse physiological stress physiology protein synthesis protein tertiary structure rat ultrastructure Mammalia Animals Cercopithecus aethiops COS Cells Cytoplasmic Granules Endoplasmic Reticulum Enzyme Inhibitors Eukaryotic Initiation Factor-2 Hela Cells HSP70 Heat-Shock Proteins Humans Mice Microscopy, Confocal NIH 3T3 Cells Oxidative Stress Polyribosomes Protein Biosynthesis Protein Structure, Tertiary Rats RNA, Small Interfering RNA-Binding Proteins Stress, Physiological Thapsigargin
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00219533_v122_n4_p563_Thomas
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paperaa:paper_00219533_v122_n4_p563_Thomas
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spelling	paperaa:paper_00219533_v122_n4_p563_Thomas2023-06-12T16:43:02Z Mammalian Staufen 1 is recruited to stress granules and impairs their assembly J. Cell Sci. 2009;122(4):563-573 Thomas, M.G. Martinez Tosar, L.J. Desbats, M.A. Leishman, C.C. Boccaccio, G.L. ER stress Oxidative stress P bodies Silencing foci Staufen Stress granules initiation factor 2alpha RNA binding protein staufen 1 unclassified drug enzyme inhibitor heat shock protein 70 initiation factor 2 RNA binding protein small interfering RNA staufen protein, mammalian thapsigargin animal cell article cell granule cellular stress response controlled study endoplasmic reticulum stress gene overexpression gene silencing human human cell nonhuman oxidative stress polysome priority journal protein assembly protein phosphorylation regulatory mechanism translation initiation animal biosynthesis cell granule cell strain 3T3 cell strain COS1 Cercopithecus chemistry confocal microscopy drug effect endoplasmic reticulum HeLa cell metabolism mouse physiological stress physiology protein synthesis protein tertiary structure rat ultrastructure Mammalia Animals Cercopithecus aethiops COS Cells Cytoplasmic Granules Endoplasmic Reticulum Enzyme Inhibitors Eukaryotic Initiation Factor-2 Hela Cells HSP70 Heat-Shock Proteins Humans Mice Microscopy, Confocal NIH 3T3 Cells Oxidative Stress Polyribosomes Protein Biosynthesis Protein Structure, Tertiary Rats RNA, Small Interfering RNA-Binding Proteins Stress, Physiological Thapsigargin Stress granules are cytoplasmic mRNA-silencing foci that form transiently during the stress response. Stress granules harbor abortive translation initiation complexes and are in dynamic equilibrium with translating polysomes. Mammalian Staufen 1 (Stau1) is a ubiquitous double-stranded RNA-binding protein associated with polysomes. Here, we show that Stau1 is recruited to stress granules upon induction of endoplasmic reticulum or oxidative stress as well in stress granules induced by translation initiation blockers. We found that stress granules lacking Stau1 formed in cells depleted of this molecule, indicating that Stau1 is not an essential component of stress granules. Moreover, Stau1 knockdown facilitated stress granule formation upon stress induction. Conversely, transient transfection of Stau1 impaired stress granule formation upon stress or pharmacological initiation arrest. The inhibitory capacity of Stau1 mapped to the amino-terminal half of the molecule, a region known to bind to polysomes. We found that the fraction of polysomes remaining upon stress induction was enriched in Stau1, and that Stau1 overexpression stabilized polysomes against stress. We propose that Stau1 is involved in recovery from stress by stabilizing polysomes, thus helping stress granule dissolution. Fil:Thomas, M.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Martinez Tosar, L.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Desbats, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Boccaccio, G.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2009 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00219533_v122_n4_p563_Thomas
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
language	Inglés
orig_language_str_mv	eng
topic	ER stress Oxidative stress P bodies Silencing foci Staufen Stress granules initiation factor 2alpha RNA binding protein staufen 1 unclassified drug enzyme inhibitor heat shock protein 70 initiation factor 2 RNA binding protein small interfering RNA staufen protein, mammalian thapsigargin animal cell article cell granule cellular stress response controlled study endoplasmic reticulum stress gene overexpression gene silencing human human cell nonhuman oxidative stress polysome priority journal protein assembly protein phosphorylation regulatory mechanism translation initiation animal biosynthesis cell granule cell strain 3T3 cell strain COS1 Cercopithecus chemistry confocal microscopy drug effect endoplasmic reticulum HeLa cell metabolism mouse physiological stress physiology protein synthesis protein tertiary structure rat ultrastructure Mammalia Animals Cercopithecus aethiops COS Cells Cytoplasmic Granules Endoplasmic Reticulum Enzyme Inhibitors Eukaryotic Initiation Factor-2 Hela Cells HSP70 Heat-Shock Proteins Humans Mice Microscopy, Confocal NIH 3T3 Cells Oxidative Stress Polyribosomes Protein Biosynthesis Protein Structure, Tertiary Rats RNA, Small Interfering RNA-Binding Proteins Stress, Physiological Thapsigargin
spellingShingle	ER stress Oxidative stress P bodies Silencing foci Staufen Stress granules initiation factor 2alpha RNA binding protein staufen 1 unclassified drug enzyme inhibitor heat shock protein 70 initiation factor 2 RNA binding protein small interfering RNA staufen protein, mammalian thapsigargin animal cell article cell granule cellular stress response controlled study endoplasmic reticulum stress gene overexpression gene silencing human human cell nonhuman oxidative stress polysome priority journal protein assembly protein phosphorylation regulatory mechanism translation initiation animal biosynthesis cell granule cell strain 3T3 cell strain COS1 Cercopithecus chemistry confocal microscopy drug effect endoplasmic reticulum HeLa cell metabolism mouse physiological stress physiology protein synthesis protein tertiary structure rat ultrastructure Mammalia Animals Cercopithecus aethiops COS Cells Cytoplasmic Granules Endoplasmic Reticulum Enzyme Inhibitors Eukaryotic Initiation Factor-2 Hela Cells HSP70 Heat-Shock Proteins Humans Mice Microscopy, Confocal NIH 3T3 Cells Oxidative Stress Polyribosomes Protein Biosynthesis Protein Structure, Tertiary Rats RNA, Small Interfering RNA-Binding Proteins Stress, Physiological Thapsigargin Thomas, M.G. Martinez Tosar, L.J. Desbats, M.A. Leishman, C.C. Boccaccio, G.L. Mammalian Staufen 1 is recruited to stress granules and impairs their assembly
topic_facet	ER stress Oxidative stress P bodies Silencing foci Staufen Stress granules initiation factor 2alpha RNA binding protein staufen 1 unclassified drug enzyme inhibitor heat shock protein 70 initiation factor 2 RNA binding protein small interfering RNA staufen protein, mammalian thapsigargin animal cell article cell granule cellular stress response controlled study endoplasmic reticulum stress gene overexpression gene silencing human human cell nonhuman oxidative stress polysome priority journal protein assembly protein phosphorylation regulatory mechanism translation initiation animal biosynthesis cell granule cell strain 3T3 cell strain COS1 Cercopithecus chemistry confocal microscopy drug effect endoplasmic reticulum HeLa cell metabolism mouse physiological stress physiology protein synthesis protein tertiary structure rat ultrastructure Mammalia Animals Cercopithecus aethiops COS Cells Cytoplasmic Granules Endoplasmic Reticulum Enzyme Inhibitors Eukaryotic Initiation Factor-2 Hela Cells HSP70 Heat-Shock Proteins Humans Mice Microscopy, Confocal NIH 3T3 Cells Oxidative Stress Polyribosomes Protein Biosynthesis Protein Structure, Tertiary Rats RNA, Small Interfering RNA-Binding Proteins Stress, Physiological Thapsigargin
description	Stress granules are cytoplasmic mRNA-silencing foci that form transiently during the stress response. Stress granules harbor abortive translation initiation complexes and are in dynamic equilibrium with translating polysomes. Mammalian Staufen 1 (Stau1) is a ubiquitous double-stranded RNA-binding protein associated with polysomes. Here, we show that Stau1 is recruited to stress granules upon induction of endoplasmic reticulum or oxidative stress as well in stress granules induced by translation initiation blockers. We found that stress granules lacking Stau1 formed in cells depleted of this molecule, indicating that Stau1 is not an essential component of stress granules. Moreover, Stau1 knockdown facilitated stress granule formation upon stress induction. Conversely, transient transfection of Stau1 impaired stress granule formation upon stress or pharmacological initiation arrest. The inhibitory capacity of Stau1 mapped to the amino-terminal half of the molecule, a region known to bind to polysomes. We found that the fraction of polysomes remaining upon stress induction was enriched in Stau1, and that Stau1 overexpression stabilized polysomes against stress. We propose that Stau1 is involved in recovery from stress by stabilizing polysomes, thus helping stress granule dissolution.
format	Artículo Artículo publishedVersion
author	Thomas, M.G. Martinez Tosar, L.J. Desbats, M.A. Leishman, C.C. Boccaccio, G.L.
author_facet	Thomas, M.G. Martinez Tosar, L.J. Desbats, M.A. Leishman, C.C. Boccaccio, G.L.
author_sort	Thomas, M.G.
title	Mammalian Staufen 1 is recruited to stress granules and impairs their assembly
title_short	Mammalian Staufen 1 is recruited to stress granules and impairs their assembly
title_full	Mammalian Staufen 1 is recruited to stress granules and impairs their assembly
title_fullStr	Mammalian Staufen 1 is recruited to stress granules and impairs their assembly
title_full_unstemmed	Mammalian Staufen 1 is recruited to stress granules and impairs their assembly
title_sort	mammalian staufen 1 is recruited to stress granules and impairs their assembly
publishDate	2009
url	http://hdl.handle.net/20.500.12110/paper_00219533_v122_n4_p563_Thomas
work_keys_str_mv	AT thomasmg mammalianstaufen1isrecruitedtostressgranulesandimpairstheirassembly AT martineztosarlj mammalianstaufen1isrecruitedtostressgranulesandimpairstheirassembly AT desbatsma mammalianstaufen1isrecruitedtostressgranulesandimpairstheirassembly AT leishmancc mammalianstaufen1isrecruitedtostressgranulesandimpairstheirassembly AT boccacciogl mammalianstaufen1isrecruitedtostressgranulesandimpairstheirassembly
_version_	1769810215952187392

Mammalian Staufen 1 is recruited to stress granules and impairs their assembly

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