Skip to main content
. Author manuscript; available in PMC: 2015 Oct 1.
Published in final edited form as: J Cell Physiol. 2014 Oct;229(10):1529–1537. doi: 10.1002/jcp.24596

Figure 9. ERK3 enhances the interactions of SRC3 with CBP and SP1.

Figure 9

(A) and (B). Cells were co-transfected with SRC-3Flag and ERK3 or the corresponding empty vector. The interactions of SRC-3 with CBP and SP1 were analyzed by immunoprecipitation (IP) using a Flag Ab or a mouse IgG, followed by Western blotting. The relative SRC-3 binding capacity with CBP or SP1 was determined by measuring the CBP or SP1 immunoblot (IB) band intensity in the IP samples. The band intensity in control vector group was arbitrarily set as “1.0”. Overexpression of ERK3 (A) enhanced the interactions of SRC-3 with CBP and SP1 shown in (B). (C) and (D). Cells were transfected with ERK3 siRNA (ERK3si) or the silencer negative control siRNA (Ctrlsi), together with SRC-3Flag plasmid. The interactions of SRC-3 with CBP and SP1 were analyzed by IP using a Flag Ab, followed by Western blotting. Numbers below the immunoblots of CBP and SP1 in Flag Ab/IP samples represent the relative SRC-3 binding capacity with these proteins, which is determined by the ratio of the band intensity in Flag Ab/IP over that in the corresponding input. For the purpose of comparison, the relative binding capacity (the ratio) in Ctrlsi group was arbitrarily set as “1.0”. Knockdown of ERK3 (C) greatly decreased the association of SRC3 with CBP and SP1 (D).