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RhoA activation participates in rearrangement of processing bodies and release of nucleated AU-rich mRNAs

Cytoplasmic ribonucleoprotein granules, known as processing bodies (P-bodies), contain a common set of conserved RNA-processing enzymes, and mRNAs with AU-rich elements (AREs) are delivered to P-bodies for translational silencing. Although the dynamics of P-bodies is physically linked to cytoskeleta...

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Detalles Bibliográficos
Autores principales: Takahashi, Shinya, Sakurai, Kyoko, Ebihara, Arisa, Kajiho, Hiroaki, Saito, Kota, Kontani, Kenji, Nishina, Hiroshi, Katada, Toshiaki
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2011
Materias:
RNA
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3082882/
https://www.ncbi.nlm.nih.gov/pubmed/21212127
http://dx.doi.org/10.1093/nar/gkq1302
Descripción
Sumario:Cytoplasmic ribonucleoprotein granules, known as processing bodies (P-bodies), contain a common set of conserved RNA-processing enzymes, and mRNAs with AU-rich elements (AREs) are delivered to P-bodies for translational silencing. Although the dynamics of P-bodies is physically linked to cytoskeletal network, it is unclear how small GTPases are involved in the P-body regulation and the ARE-mRNA metabolism. We found here that glucose depletion activates RhoA GTPase and alters the P-body dynamics in HeLa cells. These glucose-depleted effects are reproduced by the overexpression of the RhoA-subfamily GTPases and conversely abolished by the inhibition of RhoA activation. Interestingly, both RhoA activation and glucose depletion inhibit the mRNA accumulation and degradation. These findings indicate that RhoA participates in the stress-induced rearrangement of P-bodies and the release of nucleated ARE-mRNAs for their stabilization.