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

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 ra...

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Autor principal: Loschi, Mariela
Publicado: 2009
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219533_v122_n21_p3973_Loschi
http://hdl.handle.net/20.500.12110/paper_00219533_v122_n21_p3973_Loschi
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spelling paper:paper_00219533_v122_n21_p3973_Loschi2023-06-08T14:43:42Z Dynein and kinesin regulate stress-granule and P-body dynamics Loschi, Mariela 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 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. 2009 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219533_v122_n21_p3973_Loschi http://hdl.handle.net/20.500.12110/paper_00219533_v122_n21_p3973_Loschi
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
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
spellingShingle 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
Loschi, Mariela
Dynein and kinesin regulate stress-granule and P-body dynamics
topic_facet 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
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.
author Loschi, Mariela
author_facet Loschi, Mariela
author_sort Loschi, Mariela
title Dynein and kinesin regulate stress-granule and P-body dynamics
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
publishDate 2009
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219533_v122_n21_p3973_Loschi
http://hdl.handle.net/20.500.12110/paper_00219533_v122_n21_p3973_Loschi
work_keys_str_mv AT loschimariela dyneinandkinesinregulatestressgranuleandpbodydynamics
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