Research Article

Functional Differences between the N-Terminal Domains of Mouse and Human Myosin Binding Protein-C

Figure 3

Effects of mouse and human C0, P/A, and C1 domains on motility of regulated thin filaments (F-actin + Tm + Tn) at pCa 9. (a) Compared to control experiments in the absence of added protein ( 𝑛 = 12), 1  𝜇 M hC0C1 significantly activated filament sliding speed motility and the fraction of filaments moving ( 𝑛 = 8), whereas 1  𝜇 M mC0C1 did not affect motility ( 𝑛 = 9). (b) Substitution of the human for mouse P/A domain in the mouse C0C1 backbone (mhmC0C1) activated motility ( 𝑛 = 7), whereas substitution of the mouse P/A domain into the human backbone (hmhC0C1) depressed motility relative to hC0C1 ( 𝑛 = 5). (c) Exchange of mouse and human C1 domains. The human C1 domain (mmhC0C1) activated motility (compared to mC0C1, 𝑛 = 5), whereas the mouse C1 domain (hhmC0C1) depressed motility (compared to hC0C1, 𝑛 = 6). (d) Exchange of mouse and human C0 domains. The human C0 (hmmC0C1, 𝑛 = 5) and mouse C0 (mhhC0C1, 𝑛 = 10) domains did not affect thin filament motility (compared to mC0C1 and hC0C1 controls, resp.). Data are mean ± SD. Asterisks (*) and crosses (†) denote significant differences compared to mC0C1 and hC0C1, respectively, ( 𝑃 < . 0 5 ).
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