IndraLab

Statements

TGFBR1 binds USP11. 12 / 12
1 | 6 5
reach
"USP11 may bind ALK5 and prevent the SMAD7-E3 ligase complex access to ubiquitylate the receptor."
22773947
reach
"In the case of USP11, SMAD7 does not appear to act exclusively as a scaffold for as SMAD7 does not appear to mediate the interaction between USP11 and TbetaRI, despite the fact that SMAD7 and USP11 be[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
28923280
reach
"FLAG-ALK5 interacted with HA-USP11, and this interaction was only slightly enhanced in the presence of over-expressed SMAD7 (XREF_FIG a)."
22773947
reach
"However, because USP11 interacts with ALK5 and positively regulates the TGFbeta pathway dependent on its catalytic activity, ALK5 appeared to be a strong candidate for deubiquitylation by USP11."
22773947
reach
"USP11 interacts with ALK5."
22773947
sparser
"However, because USP11 interacts with ALK5 and positively regulates the TGFβ pathway dependent on its catalytic activity, ALK5 appeared to be a strong candidate for deubiquitylation by USP11."
22773947
sparser
"USP11 interacts with ALK5."
22773947
reach
"When bound to ALK5, USP11 deubiquitylates and protects ALK5 from proteasomal degradation resulting in enhanced TGFbeta signalling."
25007997
sparser
"USP11 binds and deubiquitinates Alk5, a type I TGF-β receptor, which results in enhanced TGF-β-induced gene transcription."
33158118
biogrid
No evidence text available
22773947
sparser
"USP11 may bind ALK5 and prevent the SMAD7-E3 ligase complex access to ubiquitylate the receptor."
22773947
sparser
"In light of the USP11–ALK5 interaction, we characterized the subcellular localization of endogenous SMAD7, USP11 and ALK5 to confirm that their interactions were not an artefact of the biochemical techniques used."
22773947