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...
| Autores: | , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2009 |
| País: | Argentina |
| Institución: | Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
| Repositorio: | Biblioteca Digital (UBA-FCEN) |
| Idioma: | inglés |
| OAI Identifier: | paperaa:paper_00219533_v122_n21_p3973_Loschi |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00219533_v122_n21_p3973_Loschi |
| Access Level: | acceso abierto |
| Palabra clave: | 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 Mice Microtubule-Associated Proteins NIH 3T3 Cells Protein Biosynthesis Mammalia |
| Sumario: | 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. |
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