The differences in the ability of Ynd1 mutants to mediate E4orf4-induced toxicity could possibly reflect altered subcellular localizations.
On the other hand, the abilities of S184A/T282A and S184D/T282E ZBTB16 mutants to mediate the ubiquitination of Atg14L were higher and lower than that of wt, respectively.
First, the ability of N279D mutant tau to mediate polymerization of tubulin was compared to that of wild-type tau by monitoring the turbidity after mixing tubulin with tau.
As seen previously, the Y699F STAT5b mutant was unable to mediate STAT5b transcriptional activity, and the addition of Brk had no effect.
These data indicate that the human ALKF1174I mutant is able to mediate neurite outgrowth, transform NIH3T3 cells, activate downstream targets of ALK (such as ERK and STAT3) in a ligand-independent manner and substitute for IL-3 in Ba/F3 cells, giving rise to IL-3-independent cell line.
Neither of the mutants was able to mediate TBP ubiquitination in vitro.
Likewise, the ALKM1166R and ALKF1174I mutants were able to mediate neurite outgrowth in PC12 cells in a ligand-independent manner (Table 1).
Figure 2A demonstrates that most mutants were able to mediate uptake of both OATP-model substrates estrone-3-sulfate and estradiol-17β-glucuronide. Transport of each substrate was negligible in each of the mutants F534C, F537C, Q541C, and A549C.
We transfected Agt5 −/− MEF cells with wild-type p62 or a LIR deletion mutant, which was reported to mediate its interaction with LC3 for autophagic degradation, and found that the protein level of p62 or its LIR deletion mutant were significantly reduced when parkin is expressed in these cells (Fig. 3C).
However, overexpression of Cdc6 in mutant Bmi1 cells failed to mediate Arf or Ink4a repression (Fig. 4A,D) demonstrating that CDC6 induced repression of the INK4a/ARF locus is dependent on Polycomb function.
