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RhoA activation participates in rearrangement of processing bodies and release of nucleated AU-rich mRNAs.
- Source :
-
Nucleic acids research [Nucleic Acids Res] 2011 Apr; Vol. 39 (8), pp. 3446-57. Date of Electronic Publication: 2011 Jan 06. - Publication Year :
- 2011
-
Abstract
- 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.
- Subjects :
- Adenine analysis
Animals
Cytoplasmic Granules chemistry
Cytoplasmic Granules metabolism
Glucose physiology
HeLa Cells
Humans
Mice
NIH 3T3 Cells
RNA, Messenger chemistry
Ribonucleoproteins analysis
Tristetraprolin metabolism
Uracil analysis
RNA Processing, Post-Transcriptional
RNA, Messenger metabolism
rhoA GTP-Binding Protein metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1362-4962
- Volume :
- 39
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Nucleic acids research
- Publication Type :
- Academic Journal
- Accession number :
- 21212127
- Full Text :
- https://doi.org/10.1093/nar/gkq1302