Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation.

Molecular and Cellular Biochemistry
Shan LiLingqiang Zhang

Abstract

The HECT-type E3 Smad ubiquitination regulation factor 1 (Smurf1) functions in regulation of cell polarity and bone homeostasis by targeting Smads, Runx2, RhoA and MEKK2 for ubiquitination and degradation. In a yeast two-hybrid screening, we identified TNF receptor-associated factor 4 (TRAF4) as a candidate substrate and was further validated. The PY motifs of TRAF4 mediated the interaction with the second WW domain of Smurf1. Overexpression of Smurf1 reduced the protein levels of TRAF4 dependent of its E3 activity and the proteasome. Further, we showed that all six members of TRAF family could be ubiquitinated by Smurf1. Consequently, Smurf1 interfered with the functions of TRAFs in NF-kappaB signaling under stimulation or not. These results suggested a new role of Smurf1 in inflammation and immunity through controlling the degradation of TRAFs.

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Citations

Jul 11, 2019·Journal of Molecular Cell Biology·Yihao LiPeter Ten Dijke
Dec 30, 2015·The Journal of Experimental Medicine·Steven M HeatonVishva M Dixit
Mar 16, 2011·The Journal of Biological Chemistry·Kefeng LuFuchu He
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Nov 19, 2020·Cancer Gene Therapy·Qin XiaLei Dong

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