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. 2010 Aug 4;99(3):897–904. doi: 10.1016/j.bpj.2010.04.070

Figure 3.

Figure 3

Blocking of the BRIa-CK2 interaction by peptides led to Smad-dependent signaling. (A) C2C12 cells were transfected with control siRNA or with siRNA against the CK2 α-subunit. Cells were then fixed and immunofluorescently labeled for CK2 α-subunit. The fluorescent signal was measured using a confocal microscope. CK2-α expression was downregulated by 40%. The error bars depict the SD (p < 0.05). (B) Cells transfected with pSBE and pRLuc were incubated with BMP2 or peptides to block the interaction of BRIa and CK2. For the siRNA luciferase assay, plasmids encoding pSBE, pRLuc, and the CK2 α-subunit siRNA were cotransfected. Presence of the peptides or CK2-α siRNA led to BMP-independent Smad signaling (p < 0.05).