IndraLab

Statements


3 | 5 2

No evidence text available

reach
"The strong interaction between USP15 and ALK3 and their co-localization at the plasma membrane suggested that USP15 could act as a DUB for ALK3."

reach
"We show that USP15 interacts with SMAD6 and ALK3 and enhances BMP signalling by deubiquitylating ALK3 and rescuing it from proteasomal destruction."

reach
"Next, we tested how SMAD6 affected the interaction between GFP-USP15 and FLAG-ALK3 (XREF_FIG b)."

sparser
"The strong interaction between USP15 and ALK3 and their co-localization at the plasma membrane suggested that USP15 could act as a DUB for ALK3."

No evidence text available

sparser
"SMAD6 overexpression disrupts the association of USP15 with ALK3 and potently inhibits BMP signalling."

reach
"It was shown that USP15 interacts with type I BMP receptors, including ALK3, co-localises with ALK3 at the membrane and deubiquitylates ALK3, thereby countering the inhibition of the BMP pathway caused by SMAD6 XREF_BIBR."

No evidence text available

reach
"Here, we demonstrate that USP15 interacts with and deubiquitylates the type I BMP receptor ALK3."