Figure 5: P-Rex1 and Rac1 bind preferentially to the GEL and LRR domain of FLII, respectively. | Nature Communications

Figure 5: P-Rex1 and Rac1 bind preferentially to the GEL and LRR domain of FLII, respectively.

From: Differential Rac1 signalling by guanine nucleotide exchange factors implicates FLII in regulating Rac1-driven cell migration

Figure 5

(a) Schematic representation of FLII domain structure showing 16 leucine-rich repeats (LRR) comprising the N-terminal LRR domain and six gelsolin-like repeats (S1-S6) representing the C-terminal GEL domain together with the amino acid number (a.a. #) range for each domain. FLII FL, full-length FLII; FLII GEL, gelsolin domain only; FLII LRR, LRR domain only. (b) FLAG immunoprecipitation (IP) from HEK293T cells expressing the different FLAG-tagged FLII domain mutants outlined in a alone or together with P-Rex1 WT. Co-precipitated exogenous P-Rex1 was detected by western blot analysis. α-Tubulin was used as a loading control. Representative western blot from three independent experiments. (c) GST pulldown using purified GST (EV) or GST-tagged Rac1 WT (Rac1 WT) loaded with GTPγS and incubated with HEK293T lysates expressing the different FLAG-tagged FLII domain mutants outlined in a. Co-precipitated FLAG-tagged FLII domain mutants were detected by western blot analysis. Ponceau staining was used as a loading control. Representative western blot from three independent experiments.

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