IndraLab

Statements

SMAD7 binds USP15. 16 / 21
3 | 6 7
sparser
"Thus, the intensity of TGF-β could directly influence the formation of the USP15-SMAD7 complex."
30980801
reach
"TGF-β activity in GBM is modulated by several deubiquitinating enzymes (DUBs); first, it was described that TGF-β activity could be enhanced due to the amplification of a deubiquitinating enzyme, USP15, which binds to the SMAD7–SMURF2 complex and stabilizes type I TGF-β receptors, resulting in enhanced TGF-β signaling."
38256140
biogrid
No evidence text available
22344298
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
"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."
22921829
reach
"USP15 binds to the SMAD7–SMAD E3 ligase complex and deubiquitinates and stabilizes the type I TGF-β receptor (TGFβR-I), leading to an enhanced TGF-β signal."
25444757
reach
"Combined with the above results showing that USP15 forms a complex with SMAD7, we hypothesized that USP15 could be recruited to TBR1 by SMAD7."
30980801
sparser
"Combined with the above results showing that USP15 forms a complex with SMAD7, we hypothesized that USP15 could be recruited to TBR1 by SMAD7."
30980801
sparser
"USP15 also binds to SMAD7, forming a complex with SMURF2 that negatively regulates TGF-β."
34124032
biogrid
No evidence text available
30980801
sparser
"Conclusively, our results illustrate that USP15 binds to SMAD7 and deubiquitinates TBR1, stabilizing the TBR1 structure."
30980801
reach
"Conclusively, our results illustrate that USP15 binds to SMAD7 and deubiquitinates TBR1, stabilizing the TBR1 structure."
30980801
biogrid
No evidence text available
36213818
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
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