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. 2021 Jan 19;10(1):66. doi: 10.3390/biology10010066

Figure 2.

Figure 2

Tristetraprolin (TTP) protein structure, activity regulation, and function. (a) p38-MAPK activates MK2, which phosphorylates TTP at serines 52 and 178 (mouse), which allows for binding of 14-3-3 and inactivation of TTP. DUSP 1 inhibits p38-MAPK. (NES: nuclear export signal; NOT1 BD: NOT1 binding domain) (b) TTP interacts with adenosine and uridine (AU)-rich elements (AREs) in the 3′ untranslated region of target mRNAs and recruits the CCR4-NOT deadenylation complex, facilitating rapid degradation of the target mRNA. (ORF: open reading frame).