Fig. 6: Mutational analysis of UBXD1. | Nature Structural & Molecular Biology

Fig. 6: Mutational analysis of UBXD1.

From: The p97/VCP adaptor UBXD1 drives AAA+ remodeling and ring opening through multi-domain tethered interactions

Fig. 6

a, Schematic of UBXD1 mutants tested. b, Steady-state ATPase activity of p97 as a function of UBXD1 protein concentration for WT (wild type), LX (lariat mutant: E299R/R302E/R307E/E312R) or H4X (helix H4 sequence scramble) (normalized to activity at 0 nM UBXD1). Dashed lines represent the minimal activity (or maximal UBXD1 inhibition) obtained from the corresponding curve fit. Data are from n = 3 independent experiments, each with three technical replicates. Data are presented as mean values from each independent experiment. c, As in b, but for UBXD1-N (residues 1–133), UBXD1-C (residues 94–end) or an equimolar combination of UBXD1-N and UBXD1-C. Data are from n = 3 independent experiments, each with three technical replicates. Data are presented as mean values from each independent experiment. d Calculated IC50 values for ATPase inhibition by UBXD1 mutants. Data are from n = 3 independent experiments, each with three technical replicates. Error bars, 95% CI; ND, not determined.

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