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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_00219533_v122_n21_p3973_Loschi
Ver los metadatos del registro completo
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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/ar2025-09-29T13:43:03Zpaperaa: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:18962025-09-29 13:43:04.416Biblioteca 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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1844618738171641856 |
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13.070432 |