Members of this protein family regulate pre-mRNA alternative splicing and may also be involved in mRNA editing, and translation.

[10] Human CUGBP1 (hCUGBP1) had been previously identified by Timchenko and colleagues[5] for its ability to bind to CUG repeats located in the DMPK 3'UTR.

Years ago, it was shown that the class III ARE (devoid of any AUUUA motif) of the human c-jun oncogene directed rapid deadenylation and degradation to a reporter mRNA.

This was recently demonstrated by siRNA-mediated knockdown of hCUGBP1 that led to stabilization of a reporter RNA bearing the c-jun UG -rich ARE.

A SELEX approach for the identification of artificial substrate of hCUGBP1 led to the proposition that UGU containing sequences were highly favoured for binding.

[19] Such a motif is found in a number of unstable mRNAs in human cells[17] suggesting that they are degraded by a CUGBP1 deadenylation dependent pathway.