Key result
Beta-actin mutations P38A and C374S interfered with actin polymerization and myosin interaction, with C374S also abolishing profilin binding and reducing filament motility in vitro.
Population
Beta-actin mutants (P38A and C374S) and wild-type beta-actin expressed in S. cerevisiae
Comparison
P38A and C374S mutations in beta-actin vs Wild-type beta-actin
Design
Preclinical
Authors
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Results from this in vitro study should not change clinical practice; leaves open functional consequences of beta-actin mutations in patients.
Mutations in beta-actin (P38A and C374S) disrupt actin polymerization and interactions with myosin and profilin in vitro.
Aspenström et al. (1993) studied this question. Beta-actin mutants (P38A and C374S) vs. Wild-type beta-actin was evaluated on Polymerizability and interaction with DNase I, myosin, and profilin. Beta-actin mutations P38A and C374S interfered with actin polymerization and myosin interaction, with C374S also abolishing profilin binding and reducing filament motility in vitro.
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