IndraLab

Statements

USP15 binds SMURF2. 9 / 12
3 | 5 1
reach
"Initially, we tested if mutated SMURF2 could form complexes with both SMAD7 and USP15."
26435193
reach
"Furthermore, recent reports have identified a number of shared substrates of SMURF2 and USP15 including MDM2, SMAD3, and RNF20, suggesting that the association between SMURF2 and USP15 may serve as a common regulatory method to control multiple analogous cellular protein complexes XREF_BIBR XREF_BIBR XREF_BIBR XREF_BIBR XREF_BIBR XREF_BIBR."
26435193
biogrid
No evidence text available
26435193
reach
"As shown in XREF_FIG, mutated SMURF2 bound to both USP15 and SMAD7 to the same degree as wild type SMURF2."
26435193
biogrid
No evidence text available
26435193
reach
"Using a functional genetic screen we have previously found that USP15 forms a complex with SMAD7 and SMURF2 and is recruited to the TGF-beta receptor complex, where it deubiquitinates and stabilizes TbetaRI XREF_BIBR."
26435193
biogrid
No evidence text available
22344298
sparser
"USP15 binds to Smurf2 complex and deubiquitinates and stabilizes TRβ1, and that apparently leads to boosting of TGF-β-mediated signaling."
25885904
reach
"USP15 binds to Smurf2 complex and deubiquitinates and stabilizes TRbeta1, and that apparently leads to boosting of TGF-beta-mediated signaling."
25885904