IndraLab
Statements
sparser
"The above analysis has indicated the importance of the N-terminal 14 amino acids on YAP and the amino acid stretch 34-146 on EIF3H in mediating the interaction between YAP and EIF3H. To further identify the pivotal amino acid residues in EIF3H responsible for recognition of YAP by EIF3H, we have further performed molecular docking simulations by homology modelling service iTASSER and Haddock ( xref – xref )."
sparser
"As shown in xref – xref , replacement of Trp119, Tyr140 alone or combine by alanines significantly destabilized EIF3H-binding to YAP, presumably due to the perturbation of the interfacial interactions between EIF3H and YAP ( xref ), and reduced the deubiquitylation capacity of EIF3H, which function same as the catalytic core mutant EIF3H DDQ/AAA ( xref )."
sparser
"To our surprise, we observed, while only overexpression of the wild-type EIF3H fully recapitulates lung metastasis, the expression of mutant EIF3H fails to restore lung metastasis, indicating that EIF3H-YAP axis is critical for EIF3H-driven tumor invasion and metastasis ( xref and xref )."
sparser
"To determine the impact of W119 and Y140 on EIF3H in mediating the interaction between EIF3H with YAP, we have engineered double point mutant EIF3H constructs replacing by alanine (W119A and Y140A), and further tested the impact of these point mutations of EIF3H on altering the ubiquitylation and degradation of the substrate YAP."