TTP interacts directly with exonucleases (XRN1 and the exosome) and decapping enzymes (DCP1a and DCP2) which hydrolyze the mRNA bound by TTP. TTP also recruits PARN deadenylase, however a direct interaction between TTP and PARN has not been demonstrated.
Tristetraprolin (TTP) binds UUAUUUAUU motifs in the AU-rich elements of mRNAs. TTP binds Transportin-1 (Importin beta-2) which plays a role in shuttling TTP between P-bodies and stress granules.
Phosphorylated tristetraproline (TTP) binds 14-3-3, which inhibits the ability of TTP to destabilize RNA. Thus RNAs bound by TTP become stabilized. The binding of 14-3-3 causes TTP to be excluded from stress granules.
ZFP36L2 bound to AU-rich elements of specific mRNAs recruits the CCR4-NOT complex via an interaction between ZFP36L2 and CNOT6L of the CCR4-NOT complex (inferred from mouse homologs). CNOT6L then deadenylates the mRNA, targeting the mRNA for degradation (inferred from mouse homologs).
In maturing oocytes ZFP36L2 binds AU-rich elements in specific maternal mRNAs and also CNOT6L, a catalytic component of the CCR4-NOT RNA deadenylase complex (inferred from mouse homologs). Knockout of CNOT6L prevents degradation of maternal transcripts related to translation in maturing oocytes (inferred from mouse oocytes). Depletion or knockout of ZFP36L2 causes defects in oocyte maturation (inferred from mouse oocytes) and prevents degradation of maternal mRNAs related to histone demethylation and regulation of transcription (inferred from mouse homologs), therefore ZFP36L2 is believed to regulate degradation of specific mRNAs in oocytes.