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anti-Human TNRC6C Antibodies:
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These findings reveal that despite species-specific differences in the relative strength of the PABPC1-binding sites, the interaction between GW182 proteins and PABPC1 is critical for miRNA-mediated silencing in animal cells.
The authors show that a conserved motif in the human GW182 paralog TNRC6C interacts with the C-terminal domain of polyadenylate binding protein 1 (PABC) and present the crystal structure of the complex.
Through deletion and mutagenesis, study identified the C-terminal part of TNRC6C encompassing the RRM RNA-binding motif as a key effector domain mediating protein synthesis repression by TNRC6C.
Our findings indicate that TNRC6C, is recruited to miRNA targets through an interaction between their N-terminal domain and an Argonaute protein
These results imply a complex and indirect mode of regulation of sacculation by TNRC6c, mediated in part by dynamic transcriptional repression of an inhibitor of TGFbeta family gene expression.
Plays a role in RNA-mediated gene silencing by micro- RNAs (miRNAs). Required for miRNA-dependent translational repression of complementary mRNAs by argonaute family proteins (By similarity).
trinucleotide repeat-containing gene 6C protein