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. 2020 Dec 21;40(4):e105450. doi: 10.15252/embj.2020105450

Figure 6. ESM1 associates with the ARM domain of β‐catenin.

Figure 6

  1. Nuclear and cytosolic extracts of 22Rv1‐M cells transfected with either shScramble or shCTNNB1 were prepared, and the levels of indicated proteins were detected by immunoblotting.
  2. Nuclear or cytosolic extracts of 22Rv1‐M cells were immunoprecipitated with an ESM1 antibody.
  3. Human recombinant His‐ESM1 and GST‐β‐catenin proteins were pull down with either Ni sepharose or glutathione sepharose.
  4. Upper, mapping β‐catenin regions binding to ESM1. Schematic diagram of full‐length β‐catenin and deletion mutants. Lower, mapping ESM1 regions binding to β‐catenin. Schematic diagram of full‐length ESM1 and deletion mutants.
  5. HEK293T cells were co‐transfected with the indicated β‐catenin‐Flag and ESM1‐HA constructs. Cell extracts were immunoprecipitated with Flag‐M2 agarose beads. Light chain was labeled as l.c.
  6. HEK293T cells were transfected with ESM1‐HA constructs, and pull‐down was carried out with different purified GST‐ARM fragments.
  7. HEK293T cells were transfected with the indicated ESM1‐GFP constructs. Cell extracts were pulled down with purified GST‐ARM.

Source data are available online for this figure.