IndraLab

Statements

DLL1 binds USP2. 6 / 6
| 6
sparser
"These results suggest that USP2-45 binding to α 2 δ-1 promotes the de-ubiquitylation of both Ca v 1.2 and α 2 δ-1 subunits, in order to regulate the expression of Ca v 1.2 channels at the plasma membrane."
25366495
sparser
"This result suggests that the first critical event is the binding of USP2-45 to the auxiliary α 2 δ-1 subunit which may act as an anchor allowing for USP2-45 to de-ubiquitylate Ca v 1.2 channels."
25366495
sparser
"In addition, the binding of USP2-45 to α 2 δ-1 may disrupt the chaperone role of this subunit towards Ca v 1.2, leading to the reduction of Ca v 1.2 surface expression."
25366495
sparser
"However, USP2-45 specifically interacts with α 2 δ-1 rather than with the Ca V 1.2 channel or β 2 -subunit, thus it is not appropriate to define USP2-45 as a deubiquitinase of the Ca V 1.2 channel."
40660291
sparser
"Unexpectedly, the α 2 δ-1-USP2-45 protein interaction appears to downregulate the total expression of Ca V 1.2, α 2 δ-1 and β 2 subunits, and simultaneously to inhibit plasma membrane insertion and Ca 2+ current density of Ca V 1.2 channels in transfected HEK 293 cells."
40660291
sparser
"Though the reason for this peculiarity is presently unknown, it may lie in the fact that the USP2-45 binding to Ca V α 2 δ-1 might disrupt the chaperone role of the auxiliary subunit, leading to a reduction of the Ca V 1.2α 1 pore-forming subunit trafficked to the plasma membrane [ xref ]."
28957379