Sentence examples for binding to the cue from inspiring English sources

Furthermore, htt competes with polyubiquitin binding to the cue domain.

These results are consistent with the previous reports that polyubiquitin binding to the cue domain of gp78 is essential for gp78's function in ERAD [56], [57].

However, due to the insolubility of HEAT 2 fragment, we were not able to determine whether HEAT 2 is sufficient for binding to the cue domain.

Mutant htt compromises gp78's function in ERAD and triggers ER stress by directly binding to the cue domain, which results in inhibition of gp78 interaction with polyubiquitinated proteins and p97/VCP.

Our findings suggest that perturbation of gp78 function occurs by three interrelated mechanisms: 1) polyglutamine expansion enhances mutant htt interaction with the cue domain of gp78, thereby severely hindering polyubiquitin binding to the cue domain; 2) mutant htt sterically blocks p97/VCP interaction with gp78; 3) accumulation of mutant htt causes aggregation of gp78.

As shown in Figure 5A, polyubiquitin binding to the cue-m was significantly reduced, but was not abolished, compared to the binding seen with the wild type and CD1/2 mutant proteins (Fig. 5A, upper panel).

To obtain evidence in support of this idea, we asked whether htt inhibits ubiquitin-binding to the cue domain in a competition experiment.

Thus, the reduced binding of polyubiquitinated proteins to the cue domain in httN138Q-containing lysates may be resulted from the increased binding of httN to the cue domain due to polyglutamine expansion.

Consistent with our prediction, polyubiquitin binding to GST-cue was diminished in a polyglutamine dependent manner (Fig. 6).

Because this proline residue is essential for monoubiquitin binding, whether the CUE domain in these proteins remains as a component of the ubiquitination machinery remains to be determined.

We found that htt and ubiquitin may share the same binding residues in the cue domain.