IndraLab

Statements

USP2 deubiquitinates LDLR. 4 / 4
| 4
reach
"The authors attempt to answer this question by introducing a tripartite complex model, in which USP2 interacts with LDLR at the plasma membrane in an IDOL dependent manner to deubiquitylate and stabilize both LDLR and IDOL."
26846634
reach
"Such a temporal expression pattern would leave little opportunity to alleviate the USP2 mediated antagonism of IDOL, and the tripartite complex model would imply that IDOL is constantly engaged in a futile reaction, in which its ubiquitylation of LDLR is immediately reversed by USP2."
26846634
reach
"We identify a tri and partite complex encompassing IDOL, USP2, and LDLR and demonstrate that in this context USP2 promotes deubiquitylation of the LDLR and prevents its degradation."
26666640
reach
"In summary, USP2 activity leads to the deubiquitylation and stabilization of cell surface LDLR in and IDOL dependent manner, but it remains uncertain exactly why such a phenomenon is accompanied by an extended IDOL protein half-life."
26846634