IndraLab

Statements


SMURF2 ubiquitinates STAMBP. 6 / 7
1 1 | 3 1

"Our results also demonstrate that <span class="match term1">AMSH</span> is ubiquitinated by <span class="match term0">Smurf2</span> E3 ligase in the presence of RNF11 and that a consequent reduction in its steady-state level requires both RNF11 and <span class="match term0">Smurf2</span>"

sparser
"The protein levels of AMSH decrease in presence of both RNF11 and SMURF2, and AMSH is ubiquitinated by SMURF2 in the presence of RNF11."

"RNF11 recruits AMSH to Smurf2 E3 ligase. Smurf2 promotes ubiquitination of AMSH in the presence of wt RNF11. Previously, we have shown that RNF11 interacts with the HECT-type E3 ligases AIP4 and Smurf2. Here, we show that RNF11 binds to AMSH in mammalian cells and that this interaction is independent of the RNF11 RING-finger domain and the PY motif. Our results also demonstrate that AMSH is ubiquitinated by Smurf2 E3 ligase in the presence of RNF11 and that a consequent reduction in its steady-state level requires both RNF11 and Smurf2. RNF11 therefore recruits AMSH to Smurf2 for ubiquitination, leading to its degradation by the 26S proteasome."

reach
"Li and Seth [58] have demonstrated that AMSH itself is ubiquitinated by Smurf2, the E3 ligase that is responsible for TGF-β receptor and I-Smad ubiquitination and degradation."

reach
"Our results also demonstrate that AMSH is ubiquitinated by Smurf2 E3 ligase in the presence of RNF11 and that a consequent reduction in its steady-state level requires both RNF11 and Smurf2."

reach
"An RNF11 : Smurf2 complex mediates ubiquitination of the AMSH protein."