The RNA-induced silencing complex contains an Argonaute (AGO) protein, whose PAZ domain binds the 3' end of the miRNA. The PIWI domain of AGO is responsible for cleavage of target RNAs, that is, RNAs complementary to the miRNA. Only AGO2 (EIF2C2) is capable of cleavage, however. AGO1 (EIF2C1), AGO3 (EIF2C3), and AGO4 (EIF2C4) repress translation of target RNAs by binding without cleavage. In vivo, cleavage by AGO2 and repression of translation by all AGOs require interaction with a TNRC6 protein (GW182 protein) and MOV10. The interaction with TNRC6 proteins is also responsible for localizing the AGO complex to Processing Bodies (P-bodies). Tethering of the C-terminal domain of a TNRC6 protein to a mRNA is sufficient to cause repression of translation.