IndraLab

Statements

USP15 binds SMURF2 and SMAD7. 9 / 9
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sparser
"As shown in xref , mutated SMURF2 bound to both USP15 and SMAD7 to the same degree as wild type SMURF2."
26435193
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
"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, which recruits USP15 to TGFβ receptor I and stabilizes it without direct binding [ xref ]."
25606592
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
"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-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 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