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It is intriguing that the HK2-T473D mutant fails to bind Akt efficiently.
Aside from the facts that pericentromeres and mat contain nearly identical sequences and bind the same set of proteins4,5, a dcr1− swi6− double mutant fails to initiate and maintain mat silencing8.
Another ablation-induced failure in retraction can phenocopy mys mutants, and does so by targeting amnioserosa cells in the same region where the mutant fails to adhere to the germ band.
The L163D mutant fails to dimerize [6].
These analyses confirmed that the ΔBAR1 mutant fails to generate GlcCer (Fig. 5B).
Interestingly, these pull-down experiments showed that the mutant fails to interact with OSM.
Similar(19)
Indeed, compared to WT USP15, USP15 S678A mutant failed to translocate into nuclei following IR (Supplementary Fig. 5b, c).
Introducing a point mutation in the STIM1 Ca(2+) binding domain resulted in prelocalization of the protein in puncta, and this mutant failed to respond to store depletion.
Mechanistically, USP15 S678A mutant failed to deubiquitinate BARD1 in response to MMC treatment, and in turn failed to facilitate the interaction between BARD1 and HP1γ (Supplementary Fig. 5f, g).
(d) The N51A mutant failed to deaminate C due to (1) insufficient stabilization of the pyrimidine ring and (2) the lack of an ssDNA backbone anchoring.
Importantly, overexpression of wild-type TRIM28 in these cells fully abolished TRIM24 ubiquitination by both exogenous and endogenous SPOP, while TRIM28-ΔN mutant failed to rescue.
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