Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 14, Issue 6, Pages 511-518Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1249
Keywords
-
Funding
- NCI NIH HHS [R01 CA052443, R01 CA052443-14, CA052443] Funding Source: Medline
Ask authors/readers for more resources
(A+U)-rich elements (AREs) within 3 untranslated regions are signals for rapid degradation of messenger RNAs encoding many oncoproteins and cytokines. The ARE-binding protein AUF1 contributes to their degradation. We identified MYC proto-oncogene mRNA as a cellular AUF1 target. Levels of MYC translation and cell proliferation were proportional to AUF1 abundance but inversely proportional to the abundance of the ARE-binding protein TIAR, a MYC translational suppressor. Both AUF1 and TIAR affected MYC translation via the ARE without affecting mRNA abundance. Altering association of one ARE-binding protein with MYC mRNA in vivo reciprocally affected mRNA association with the other protein. Finally, genetic experiments revealed that AUF1 and TIAR control proliferation by a MYC-dependent pathway. Together, these observations suggest a novel regulatory mechanism where tuning the ratios of AUF1 and TIAR bound to MYC mRNA permits dynamic control of MYC translation and cell proliferation.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available