Key result
Saccharomyces cerevisiae CAP binds with strong preference to ADP-G-actin (Kd 0.02 µM) compared with ATP-G-actin (Kd 1.9 µM) and competes directly with cofilin for binding ADP-G-actin.
CAP preferentially binds ADP-actin monomers over ATP-actin, competing with cofilin to facilitate rapid nucleotide exchange and actin filament assembly.
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No immediate clinical implications; extends yeast actin models but leaves mammalian cardiac translation open.
Mattila et al. (2004) studied this question. Srv2/CAP was evaluated on Binding affinity to ADP-G-actin. Saccharomyces cerevisiae CAP binds with strong preference to ADP-G-actin (Kd 0.02 µM) compared with ATP-G-actin (Kd 1.9 µM) and competes directly with cofilin for binding ADP-G-actin.
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