Figure S1.
Ptsn regulates the phosphorylation of cofilin and VASP. (A–C) 293A cells were transduced with a lentivirus encoding a shRNA against Ptsn. A scrambled shRNA was used as a negative control. (A) Cell lysates were separated by SDS-PAGE and immunoblotted with an anti-phospho Ser(3) cofilin. (B) VASP was captured by immunoprecipitation (IP) and immunoblotted with an anti-phospho Ser(157) VASP. (C) Ptsn-silenced cells were transfected with a plasmid encoding either Flag-tagged α- or β-Ptsn isoforms, and phosphorylation of endogenous cofilin or VASP was assessed as described in A and B, respectively. (D and E) Phosphorylation of endogenous cofilin or VASP lysates of splenocytes isolated from WT or Ppp1r18−/− mice analyzed as described in A and B. Results are representative of three independent experiments. Source data are available for this figure: SourceData FS1.

Ptsn regulates the phosphorylation of cofilin and VASP. (A–C) 293A cells were transduced with a lentivirus encoding a shRNA against Ptsn. A scrambled shRNA was used as a negative control. (A) Cell lysates were separated by SDS-PAGE and immunoblotted with an anti-phospho Ser(3) cofilin. (B) VASP was captured by immunoprecipitation (IP) and immunoblotted with an anti-phospho Ser(157) VASP. (C) Ptsn-silenced cells were transfected with a plasmid encoding either Flag-tagged α- or β-Ptsn isoforms, and phosphorylation of endogenous cofilin or VASP was assessed as described in A and B, respectively. (D and E) Phosphorylation of endogenous cofilin or VASP lysates of splenocytes isolated from WT or Ppp1r18−/− mice analyzed as described in A and B. Results are representative of three independent experiments. Source data are available for this figure: SourceData FS1.

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