Dynein and kinesin regulate stress-granule and P-body dynamics

Autores
Loschi, M.; Leishman, C.C.; Berardone, N.; Boccacio, G.L.
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Stress granules (SGs) and P-bodies (PBs) are related cytoplasmic structures harboring silenced mRNAs. SGs assemble transiently upon cellular stress, whereas PBs are constitutive and are further induced by stress. Both foci are highly dynamic, with messenger ribonucleoproteins (mRNPs) and proteins rapidly shuttling in and out. Here, we show that impairment of retrograde transport by knockdown of mammalian dynein heavy chain 1 (DHC1) or bicaudal D1 (BicD1) inhibits SG formation and PB growth upon stress, without affecting proteinsynthesis blockage. Conversely, impairment of anterograde transport by knockdown of kinesin-1 heavy chain (KIF5B) or kinesin light chain 1 (KLC1) delayed SG dissolution. Strikingly, SG dissolution is not required to restore translation. Simultaneous knockdown of dynein and kinesin reverted the effect of single knockdowns on both SGs and PBs, suggesting that a balance between opposing movements driven by these molecular motors governs foci formation and dissolution. Finally, we found that regulation of SG dynamics by dynein and kinesin is conserved in Drosophila.
Fil:Loschi, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
J. Cell Sci. 2009;122(21):3973-3982
Materia
Bicaudal
Dynein
Kinesin
P-body
Stress granule
dynein adenosine triphosphatase
kinesin
animal cell
article
cell stress
cell structure
controlled study
dissolution
endoplasmic reticulum stress
heavy chain
light chain
molecular dynamics
nonhuman
oxidative stress
priority journal
processing bodies
protein transport
regulatory mechanism
stress granule
Animals
Cytoplasmic Structures
Dyneins
Kinesin
Mice
Microtubule-Associated Proteins
NIH 3T3 Cells
Protein Biosynthesis
Mammalia
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00219533_v122_n21_p3973_Loschi
Acceder
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oai_identifier_str paperaa:paper_00219533_v122_n21_p3973_Loschi
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Dynein and kinesin regulate stress-granule and P-body dynamicsLoschi, M.Leishman, C.C.Berardone, N.Boccacio, G.L.BicaudalDyneinKinesinP-bodyStress granuledynein adenosine triphosphatasekinesinanimal cellarticlecell stresscell structurecontrolled studydissolutionendoplasmic reticulum stressheavy chainlight chainmolecular dynamicsnonhumanoxidative stresspriority journalprocessing bodiesprotein transportregulatory mechanismstress granuleAnimalsCytoplasmic StructuresDyneinsKinesinMiceMicrotubule-Associated ProteinsNIH 3T3 CellsProtein BiosynthesisMammaliaStress granules (SGs) and P-bodies (PBs) are related cytoplasmic structures harboring silenced mRNAs. SGs assemble transiently upon cellular stress, whereas PBs are constitutive and are further induced by stress. Both foci are highly dynamic, with messenger ribonucleoproteins (mRNPs) and proteins rapidly shuttling in and out. Here, we show that impairment of retrograde transport by knockdown of mammalian dynein heavy chain 1 (DHC1) or bicaudal D1 (BicD1) inhibits SG formation and PB growth upon stress, without affecting proteinsynthesis blockage. Conversely, impairment of anterograde transport by knockdown of kinesin-1 heavy chain (KIF5B) or kinesin light chain 1 (KLC1) delayed SG dissolution. Strikingly, SG dissolution is not required to restore translation. Simultaneous knockdown of dynein and kinesin reverted the effect of single knockdowns on both SGs and PBs, suggesting that a balance between opposing movements driven by these molecular motors governs foci formation and dissolution. Finally, we found that regulation of SG dynamics by dynein and kinesin is conserved in Drosophila.Fil:Loschi, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2009info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00219533_v122_n21_p3973_LoschiJ. Cell Sci. 2009;122(21):3973-3982reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-10-23T11:18:28Zpaperaa:paper_00219533_v122_n21_p3973_LoschiInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-10-23 11:18:29.503Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Dynein and kinesin regulate stress-granule and P-body dynamics
title Dynein and kinesin regulate stress-granule and P-body dynamics
spellingShingle Dynein and kinesin regulate stress-granule and P-body dynamics
Loschi, M.
Bicaudal
Dynein
Kinesin
P-body
Stress granule
dynein adenosine triphosphatase
kinesin
animal cell
article
cell stress
cell structure
controlled study
dissolution
endoplasmic reticulum stress
heavy chain
light chain
molecular dynamics
nonhuman
oxidative stress
priority journal
processing bodies
protein transport
regulatory mechanism
stress granule
Animals
Cytoplasmic Structures
Dyneins
Kinesin
Mice
Microtubule-Associated Proteins
NIH 3T3 Cells
Protein Biosynthesis
Mammalia
title_short Dynein and kinesin regulate stress-granule and P-body dynamics
title_full Dynein and kinesin regulate stress-granule and P-body dynamics
title_fullStr Dynein and kinesin regulate stress-granule and P-body dynamics
title_full_unstemmed Dynein and kinesin regulate stress-granule and P-body dynamics
title_sort Dynein and kinesin regulate stress-granule and P-body dynamics
dc.creator.none.fl_str_mv Loschi, M.
Leishman, C.C.
Berardone, N.
Boccacio, G.L.
author Loschi, M.
author_facet Loschi, M.
Leishman, C.C.
Berardone, N.
Boccacio, G.L.
author_role author
author2 Leishman, C.C.
Berardone, N.
Boccacio, G.L.
author2_role author
author
author
dc.subject.none.fl_str_mv Bicaudal
Dynein
Kinesin
P-body
Stress granule
dynein adenosine triphosphatase
kinesin
animal cell
article
cell stress
cell structure
controlled study
dissolution
endoplasmic reticulum stress
heavy chain
light chain
molecular dynamics
nonhuman
oxidative stress
priority journal
processing bodies
protein transport
regulatory mechanism
stress granule
Animals
Cytoplasmic Structures
Dyneins
Kinesin
Mice
Microtubule-Associated Proteins
NIH 3T3 Cells
Protein Biosynthesis
Mammalia
topic Bicaudal
Dynein
Kinesin
P-body
Stress granule
dynein adenosine triphosphatase
kinesin
animal cell
article
cell stress
cell structure
controlled study
dissolution
endoplasmic reticulum stress
heavy chain
light chain
molecular dynamics
nonhuman
oxidative stress
priority journal
processing bodies
protein transport
regulatory mechanism
stress granule
Animals
Cytoplasmic Structures
Dyneins
Kinesin
Mice
Microtubule-Associated Proteins
NIH 3T3 Cells
Protein Biosynthesis
Mammalia
dc.description.none.fl_txt_mv Stress granules (SGs) and P-bodies (PBs) are related cytoplasmic structures harboring silenced mRNAs. SGs assemble transiently upon cellular stress, whereas PBs are constitutive and are further induced by stress. Both foci are highly dynamic, with messenger ribonucleoproteins (mRNPs) and proteins rapidly shuttling in and out. Here, we show that impairment of retrograde transport by knockdown of mammalian dynein heavy chain 1 (DHC1) or bicaudal D1 (BicD1) inhibits SG formation and PB growth upon stress, without affecting proteinsynthesis blockage. Conversely, impairment of anterograde transport by knockdown of kinesin-1 heavy chain (KIF5B) or kinesin light chain 1 (KLC1) delayed SG dissolution. Strikingly, SG dissolution is not required to restore translation. Simultaneous knockdown of dynein and kinesin reverted the effect of single knockdowns on both SGs and PBs, suggesting that a balance between opposing movements driven by these molecular motors governs foci formation and dissolution. Finally, we found that regulation of SG dynamics by dynein and kinesin is conserved in Drosophila.
Fil:Loschi, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description Stress granules (SGs) and P-bodies (PBs) are related cytoplasmic structures harboring silenced mRNAs. SGs assemble transiently upon cellular stress, whereas PBs are constitutive and are further induced by stress. Both foci are highly dynamic, with messenger ribonucleoproteins (mRNPs) and proteins rapidly shuttling in and out. Here, we show that impairment of retrograde transport by knockdown of mammalian dynein heavy chain 1 (DHC1) or bicaudal D1 (BicD1) inhibits SG formation and PB growth upon stress, without affecting proteinsynthesis blockage. Conversely, impairment of anterograde transport by knockdown of kinesin-1 heavy chain (KIF5B) or kinesin light chain 1 (KLC1) delayed SG dissolution. Strikingly, SG dissolution is not required to restore translation. Simultaneous knockdown of dynein and kinesin reverted the effect of single knockdowns on both SGs and PBs, suggesting that a balance between opposing movements driven by these molecular motors governs foci formation and dissolution. Finally, we found that regulation of SG dynamics by dynein and kinesin is conserved in Drosophila.
publishDate 2009
dc.date.none.fl_str_mv 2009
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_00219533_v122_n21_p3973_Loschi
url http://hdl.handle.net/20.500.12110/paper_00219533_v122_n21_p3973_Loschi
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv J. Cell Sci. 2009;122(21):3973-3982
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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score 12.982451

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