Rho activity can alter the translation of p27 mRNA and is important for RasV12-induced transformation in a manner dependent on p27 status

Vidal, Anxo, Millard, S. Sean, Miller, Jeffrey P. and Koff, Andrew (2002) Rho activity can alter the translation of p27 mRNA and is important for RasV12-induced transformation in a manner dependent on p27 status. Journal of Biological Chemistry, 277 19: 16433-16440. doi:10.1074/jbc.M112090200

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Author Vidal, Anxo
Millard, S. Sean
Miller, Jeffrey P.
Koff, Andrew
Title Rho activity can alter the translation of p27 mRNA and is important for RasV12-induced transformation in a manner dependent on p27 status
Formatted title
Rho activity can alter the translation of p27 mRNA and is important for RasV12-induced transformation in a manner dependent on p27 status
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 2002-05-10
Sub-type Article (original research)
DOI 10.1074/jbc.M112090200
Open Access Status File (Publisher version)
Volume 277
Issue 19
Start page 16433
End page 16440
Total pages 8
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
The amount of p27Kip1establishes a threshold to which G1cyclin-cyclin-dependent kinase complexes must surpass prior to cells progressing into S-phase. The amount of p27 is greatest in G0 cells, intermediate in G1 cells, and lowest in S-phase cells. However, there is little known regarding the pathways and mechanisms controlling p27 accumulation in G0 cells. We report that inhibition of Rho, by either lovastatin or C3 exoenzyme, can increase the translational efficiency of p27 mRNA. Similar pharmacologic inhibition of the phosphatidylinositol 3-kinase, the S6 kinase, and the Mek1 kinase pathways all fail to increase translational efficiency in MDA468 cells. This Rho-responsive element lies within a 300-nucleotide region at the 3′-end of the mRNA. By supporting the significance of this signaling pathway to Rho function, we showed that the suppression of RasV12 transformation by RhoAN19 is blocked in p27−/− cells. In contrast this activity is not blocked in Rb−/− orp16−/− cells. The resistance of p27−/−cells to RhoAN19 is not associated with a failure of RhoAN19 to accumulate to amounts sufficient to block Rho activity as measured by the organization of actin stress fibers. Together these results indicate a link between Rho and p27.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Biomedical Sciences Publications
 
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