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. Author manuscript; available in PMC: 2011 Jan 26.
Published in final edited form as: Biochem J. 2010 Jan 27;426(1):19–29. doi: 10.1042/BJ20090813

Figure 7. The stimulatory efficacy of polylysine on CK2 holoenzyme is reduced by the CFTRΔF peptide.

Figure 7

Calmodulin (CaM) underwent phosphorylation by CK2 holoenzyme in the absence (lane 1) or presence of either 330 nM polylysine (PL), 80 μM CFTRΔF peptide (lanes 2 and 3 respectively) or both (lane 4). The stimulatory effect of polylysine observed in lane 2 was attenuated by the CFTRΔF peptide (lane 4), which by itself is capable of enhancing phosphorylation of CaM (lane 3), albeit much less efficiently than polylysine. These results argue for a competition between polylysine and the CFTRΔF peptide for the same anchoring site.