ArticleBiophysical journal2026
In silico conformational dynamics of the α-actinin-2 actin-binding domain upon phosphorylation.
Article in Biophysical journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
In primary cardiomyocyte cell cultures, α-actinin-2 phosphorylation at the actin-binding domain (ABD) increases with mechanical stress, facilitating adaptation to varying forces. Nevertheless, it is unknown whether these phosphorylation sites in α-actinin-2 have structural consequences that could explain differential binding to F-actin and influence sarcomere stabilization and assembly. This study aims to understand the mechanisms by which α-actinin-2 regulates the assembly dynamics of sarcomeres in the heart. To investigate phosphorylation-specific modifications at the α-actinin-2 ABD, structural modeling was conducted on phosphorylation sites T43, S50, S147, and T237 alongside their phosphomimetic counterparts T43D, S50D, S147D, and T237D. We quantified conformational changes at the ABD using complementary AlphaFold3-generated models and molecular dynamics (MD) simulations of the phosphomimetic variants. AlphaFold3 modeling of phosphorylation and pseudophosphorylation sites showed an increase in the distance between the centers of mass of the two calponin homology domains (CH1 and CH2), and a decrease in torsion angles, opening the α-actinin-2 ABD. These structural changes correlated with more favorable electrostatic interaction energies (ΔH
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