Accordingly, the S59A substitution, which results in a non-phosphorylatable mutant, prevents the generation of the 59 kDa form of Lck upon iAbs stimulation.
However, in this case, addition of copper does not produce any protection, indicating that the copper-free NMBD (CXXC mutant) prevents the protective conformational change induced by the copper binding to the TMBS, as required for enzyme activation.
Ectopic expression of the WT Ezh2, but not the enzymatically inactive F667I mutant, prevents the loss of H3K27me3 and the defective adipogenesis in Ezh2−/− preadipocytes (Wang et al., 2010).
The repression of the glyoxylate cycle genes in the mutant, preventing the conversion of acetyl-CoA into oxaloacetate, may impair growth from other carbon sources, such as fatty acids.
Nevertheless, it was observed that the Aqp1b-S254A mutant prevented phosphorylation and increased Aqp1b translocation into the plasma membrane and subsequent water permeability, whereas the Aqp1b-S254D mutant, which mimicked the constitutively phosphorylated state of Aqp1b, was predominantly located in intracellular vesicles.
As shown in Figure 1D of all the mutations tested, only the W164A mutant prevented p19-RACK1 binding.
Because of the lack of resolution, we do not know if in the presence of the ARF1-locked mutant, transport intermediates were actually produced but remained in the vicinity of the donor Golgi in a coated form, or if the ARF1 mutant prevented complete formation of COPI vesicles.
In contrast, pre-infection with the eae mutant prevented IκB phosphorylation and thus degradation in response to TNFα treatment (Fig. 5A).
Importantly, blockade of Drp1 nitrosylation (using the Drp1(C644A) mutant) prevented Aβ-mediated synaptic loss and neuronal cell death, suggesting that SNO-Drp1 may represent a potential therapeutic target to protect neurons and their synapses in AD.
