Journal
JOURNAL OF CELL SCIENCE
Volume 122, Issue 21, Pages 3973-3982Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.051383
Keywords
Stress granule; P-body; Kinesin; Dynein; Bicaudal
Categories
Funding
- University of Buenos Aires [X834]
- Consejo Nacional de Investigaciones Cient ficas y Tecnologicas (CONICET) [PIP 6173]
- Agencia Nacional de Promocion Cientifica y Tecnologica, (ANPCyT), Argentina [PICT 38006, PICT 1965]
- National Institutes of Health, USA [1R03 TW 006037-01A1]
- CONICET
- Instituto Leloir
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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 protein-synthesis 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.
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