UCHL5 binds SMAD7 in complex with ubiquitinated TGFBR1

Ubiquitin C-terminal hydrolase UCHL5 (UCH37) strongly binds to SMAD7 and is thereby recruited to TGF-beta receptor complex (Wicks et al. 2005). Another ubiquitin peptidase, USP15, has recently been found to associate with ubiquitinated TGFBR1 through SMAD7 (Eichhorn et al. 2012). The role of UCHL5 was inferred from experiments using recombinant mouse Uchl5 and Smad7 with recombinant human TGF-beta receptors. The role of USP15 was established by experiments with human proteins.

泛素C端水解酶UCHL5（UCH37）与SMAD7具有强烈的结合力，因此被招募至TGF-β受体复合物中（Wicks等，2005年）。另一种泛素肽酶USP15最近被发现通过SMAD7与泛素化的TGFBR1相联系（Eichhorn等，2012年）。UCHL5的作用是通过使用重组小鼠Uchl5和Smad7以及重组人TGF-β受体进行的实验所推断出来的。USP15的作用则通过使用人源蛋白的实验得到了确立。