IndraLab

Statements

USP15 binds SMURF2 and SMAD7. 9 / 9
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sparser
"Using a functional genetic screen we have previously found that USP15 forms a complex with SMAD7 and SMURF2 and is recruited to the TGF-β receptor complex, where it deubiquitinates and stabilizes TβRI xref ."
26435193
sparser
"USP15 binds to the Smad7–SMURF2 complex, which recruits USP15 to TGFβ receptor I and stabilizes it without direct binding [ xref ]."
25606592
sparser
"USP15 binds to the SMAD7-SMAD specific E3 ubiquitin protein ligase 2 (SMURF2) complex and deubiquitinates and stabilizes type I TGF-β receptor (TβR-I), leading to an enhanced TGF-β signal."
22344298
sparser
"USP15 forms a complex with SMAD7 and SMURF2 and opposes the SMURF2-mediated ubiquitination of TβRI when the level of active TGF-β is low [ xref ]."
33946990
sparser
"Initially, we tested if mutated SMURF2 could form complexes with both SMAD7 and USP15."
26435193
sparser
"On the contrary, when the level of TGF β in the body is too low, USP15 associates with smad7 and smurf2 to form a complex to deubiquitinate the type I TGF β receptor and further increase the expression level of the intracellular signaling of TGF β [ xref , xref ]."
36213818
sparser
"As shown in xref , mutated SMURF2 bound to both USP15 and SMAD7 to the same degree as wild type SMURF2."
26435193
sparser
"At the receptor level USP15 forms a complex with SMAD7 and SMURF2 with USP15 opposing the effects of the SMURF2 ligase on TβR stabilization ."
28923280
sparser
"USP15 binds to the Smad7-Smurf2 complex and, like USP4 and USP11, deubiquitinates the TGF-β type I receptor, thereby maintaining the stability of this receptor and enhancing TGF-β signalling."
27155333