Figure 3.

Identification of interaction domains in NTRAP and TrkC. (A) Schematic representation of NTRAP mutants. (B) Yeast cells expressing the intracellular domain of TrkC fused to LexA and VP16-NTRAP mutants were streaked onto a histidine-free plate containing 10 mM 3-AT and grown at 30°C for 8 d. The number of grown yeast cells is an indicator of the interaction strength between TrkC and an NTRAP mutant. (C) Interaction of TrkC with NTRAP mutants. The #3 C₂H₂ construct is comprised of the VP16 activation domain and the third C₂H₂ zinc finger motif. The NTRAP-ZFM construct is comprised of the VP16 activation domain and an NTRAP mutant in which the two cysteine residues in the third C₂H₂ zinc finger have been changed to two alanine residues. The β-galactosidase activity in yeast two-hybrid assays reflects the interaction strength between two proteins. Error bars, SEs. **p < 0.01 by Student's t test; n = 3. (D) Interaction of NTRAP with wild-type TrkC (WT) or TrkC mutants (ΔTK and K572N). Error bars, SEs. **p < 0.01 by Student's t test; n = 3.