Figure 1 | Scientific Reports

Figure 1

From: Angulin proteins ILDR1 and ILDR2 regulate alternative pre-mRNA splicing through binding to splicing factors TRA2A, TRA2B, or SRSF1

Figure 1

ILDR1 interacts with TRA2A, TRA2B, and SRSF1. (A) Schematic drawing of the domain structures of Mus musculus ILDR1, TRA2A, TRA2B, and SRSF1. (B) Western blots showing that EGFP-tagged TRA2A, TRA2B, and SRSF1 were co-immunoprecipitated with Myc-tagged ILDR1 cytoplasmic fragment. (C) Western blots showing that EGFP-tagged ILDR1 was co-immunoprecipitated with Myc-tagged TRA2A, TRA2B, SRSF1, but not SRSF5. (D) Western blots showing that EGFP-tagged TRA2A RS domain, but not RRM domain, was co-immunoprecipitated with Myc-tagged ILDR1 cytoplasmic fragment. (E) Western blots showing that EGFP-tagged TRA2B RS domain, but not RRM domain, was co-immunoprecipitated with Myc-tagged ILDR1 cytoplasmic fragment. (F) Western blots showing that EGFP-tagged SRSF1 RS domain, but not RRM domain, was co-immunoprecipitated with Myc-tagged ILDR1 cytoplasmic fragment. Expression vectors were transfected into HEK293T cells to express epitope-tagged proteins, and cell lysis were subject to immunoprecipitation. 5% of total protein was loaded as input. IP indicates antibody used for immunoprecipitation and WB indicates antibody used for detection. Uncropped blots are shown in Fig. S9.

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