IndraLab

Statements

USP15 binds SMAD7. 7 / 12
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sparser
"To investigate how USP15 irregulates TGF- β /smad signaling in breast cancer, we first identified a strong protein interaction between USP15 and smad7, a kinase substrate of the TGF- β receptor, by experiments of coimmunoprecipitation. ( xref )."
36213818
sparser
"USP15 directly interacts with SMAD7 and other SMAD family members to deubiquitinate and stabilize type 1 TGF-β receptors, promoting TGF-β signaling ( xref , xref )."
33093067
sparser
"USP15 also binds to SMAD7, forming a complex with SMURF2 that negatively regulates TGF-β."
34124032
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
"Similar to TGF-β type I receptor associated with USP15, rather than binding to the receptor directly, USP15 binds to the receptor by SMAD7, a scaffold that also recruits SMAD-specific E3 ubiquitin protein ligase 2 (SMURF2)."
35145062
reach
"Moreover, Smad7 can simultaneously bind Smurf2 and the protein deubiquitinase USP15, recruiting both enzymes to the TGF-beta receptor complex for an integrated control of receptor polyubiquitination as a function of ligand concentration."
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