Science Advances

Supplementary Materials

The PDF file includes:

  • Fig. S1. The kinase activity of BRK and regulated signaling pathways.
  • Fig. S2. Identification of Halo-SMAD4–associated proteins.
  • Fig. S3. Activated BRK phosphorylates tyrosine-353 and tyrosine-412 on SMAD4.
  • Fig. S4. BRK and SMAD4 mRNA and protein expression in different cells.
  • Fig. S5. Halo-SMAD4/Halo-SMAD4 Y353F– and Halo-SMAD4 Y412F–associated proteins in the presence or absence of SF-BRK-YF and their ubiquitination.
  • Fig. S6. Gene ontology analyses for cellular components represented in the proteins associated with Halo-SMAD4 and phosphorylated Halo-SMAD4.
  • Fig. S7. FRK-dependent regulation of EMT markers.
  • Legends for tables S1 to S3
  • References (41, 42)

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Other Supplementary Material for this manuscript includes the following:

  • Table S1 (Microsoft Excel format). Differential protein interaction of Halo-SMAD4 in the presence of SNAP-F-BRK-WT or SNAP-F-BRK-YF (QSPEC log2 fold change, ≥1; QSPEC false discovery rate, ≤0.05).
  • Table S2 (Microsoft Excel format). Phosphorylation sites on SMAD4 detected by MudPIT analyses of in presence or absence of BRK-YF.
  • Table S3 (Microsoft Excel format). Gene ontology analysis for cellular component of Halo-SMAD4 in the presence of SNAP-F-BRK-WT or SNAP-F-BRK-YF in ClueGO FDR_0.05; Zscore_3: Tab: 3. Primers: Tab: 3.

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