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First published online 13 October 2009
doi: 10.1242/jcs.051383

Journal of Cell Science 122, 3973-3982 (2009)
Published by The Company of Biologists 2009
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Research Article

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

Mariela Loschi1,2, Claudia C. Leishman1, Neda Berardone1 and Graciela L. Boccaccio1,2,*

1 Instituto Leloir, Avenida Patricias Argentinas 435, C1405BWE-Buenos Aires, Argentina
2 Facultad de Ciencias Exactas y Naturales, University of Buenos Aires and IIBBA-CONICET, C1405BWE-Buenos Aires, Argentina

* Author for correspondence (gboccaccio{at}leloir.org.ar)

Accepted 10 September 2009

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.

Key words: Stress granule, P-body, Kinesin, Dynein, Bicaudal


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