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A more detailed translation interaction network could further refine which translation components were important in AI versus AD cells.
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Conversely, positive synergy was almost exclusively limited to translation interactions.
Translation interactions became more fragile while transcription became more robust with increasing androgen independence.
Of the statistically significant shifts, 7/9 of the cPAcP translation interactions were more sensitive in C-81.
Model analysis suggested that translation interactions were more fragile and transcription more robust in AI versus AD cells.
Predictions of this type are similar to predictions of Type I and suggest the existence of active post-translation interaction.
Although hnRNP I enhances p27 translation through interaction with the 5′-untranslated region of p27 mRNAs, interaction of UCA1 with hnRNP I suppresses p27 protein expression via competitive inhibition.
Next, we determined whether the tumor suppressor p27 serves as a potential target for UCA1 because a previous report suggested that hnRNP I interacts with p27 and enhances p27 translation through interaction with the IRES, leading to cell cycle arrest.
Although hnRNP I promotes p53 translation through interaction with the 5′-UTR of p53 mRNA, RoR may interrupt this interaction so that RoR represses p53 in response to DNA damage.
Accordingly, our proteomic results on Stau2-containing RNPs identified YB1 and PABPC1, two proteins known to modulate translation through interaction with initiation factors, as prominent candidates to fulfill translational regulation.
The indole moiety of these compounds is designed to mimic the translation stalling interaction of SecM W155 side-chain with the prokaryotic (Escherichia coli) ribosome A751 residue.
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