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Abstract:

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.

Registro:

Documento: Artículo
Título:Dynein and kinesin regulate stress-granule and P-body dynamics
Autor:Loschi, M.; Leishman, C.C.; Berardone, N.; Boccacio, G.L.
Filiación:Instituto Leloir, Avenida Patricias Argentinas 435, C1405BWE Buenos Aires, Argentina
Facultad de Ciencias Exactas y Naturales, University of Buenos Aires, IIBBA-CONICET, Buenos Aires, Argentina
Palabras 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; Kinesin; Mice; Microtubule-Associated Proteins; NIH 3T3 Cells; Protein Biosynthesis; Mammalia
Año:2009
Volumen:122
Número:21
Página de inicio:3973
Página de fin:3982
DOI: http://dx.doi.org/10.1242/jcs.051383
Título revista:Journal of Cell Science
Título revista abreviado:J. Cell Sci.
ISSN:00219533
CODEN:JNCSA
CAS:Dyneins, 3.6.4.2; Kif5b protein, mouse, 3.6.1.-; Kinesin, 3.6.1.-; Microtubule-Associated Proteins; kinesin light-chain proteins
PDF:https://bibliotecadigital.exactas.uba.ar/download/paper/paper_00219533_v122_n21_p3973_Loschi.pdf
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219533_v122_n21_p3973_Loschi

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Citas:

---------- APA ----------
Loschi, M., Leishman, C.C., Berardone, N. & Boccacio, G.L. (2009) . Dynein and kinesin regulate stress-granule and P-body dynamics. Journal of Cell Science, 122(21), 3973-3982.
http://dx.doi.org/10.1242/jcs.051383
---------- CHICAGO ----------
Loschi, M., Leishman, C.C., Berardone, N., Boccacio, G.L. "Dynein and kinesin regulate stress-granule and P-body dynamics" . Journal of Cell Science 122, no. 21 (2009) : 3973-3982.
http://dx.doi.org/10.1242/jcs.051383
---------- MLA ----------
Loschi, M., Leishman, C.C., Berardone, N., Boccacio, G.L. "Dynein and kinesin regulate stress-granule and P-body dynamics" . Journal of Cell Science, vol. 122, no. 21, 2009, pp. 3973-3982.
http://dx.doi.org/10.1242/jcs.051383
---------- VANCOUVER ----------
Loschi, M., Leishman, C.C., Berardone, N., Boccacio, G.L. Dynein and kinesin regulate stress-granule and P-body dynamics. J. Cell Sci. 2009;122(21):3973-3982.
http://dx.doi.org/10.1242/jcs.051383