SFPQ mode of binding to KLC1 is distinct from JIP1. (A) Alignment of the sequence within the C-terminal region of JIP1 containing the Y-acidic motif. Bottom: Schematic of the domains of JIP1. Red bracket indicates the region containing the Y-acidic motif. (B) Schematic cartoon depicting the location of N343 on KLC1 compared with KLC2 on the A helix of TPR4. (C) HEK 293T cells transfected with HA-SFPQ, and with either Myc-tagged WT KLC1 or KLC1N343S. HA was immunoprecipitated and blotted against HA and Myc. Input represents 0.5% of 0.5 mg of protein lysate used for HA IP, and total elute from the bead was run on the gel. JBD, JNK binding domain; PTB, phosphotyrosine binding domain; SH3, Src homology-3 domain.
Figure S3.

SFPQ mode of binding to KLC1 is distinct from JIP1. (A) Alignment of the sequence within the C-terminal region of JIP1 containing the Y-acidic motif. Bottom: Schematic of the domains of JIP1. Red bracket indicates the region containing the Y-acidic motif. (B) Schematic cartoon depicting the location of N343 on KLC1 compared with KLC2 on the A helix of TPR4. (C) HEK 293T cells transfected with HA-SFPQ, and with either Myc-tagged WT KLC1 or KLC1N343S. HA was immunoprecipitated and blotted against HA and Myc. Input represents 0.5% of 0.5 mg of protein lysate used for HA IP, and total elute from the bead was run on the gel. JBD, JNK binding domain; PTB, phosphotyrosine binding domain; SH3, Src homology-3 domain.

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