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- W2912279499 abstract "Lysine deacetylases (KDAC's) catalyze the removal of acetyl groups from lysine side chains, while lysine acetylases (KAT's) perform the reverse reaction. KDAC inhibition was shown to increase lysine acetylation of muscle proteins, and was associated with enhanced Ca2+-sensitivity in skinned fibers and increased relaxation rate in isolated myofibrils. Interestingly, the KAT enzyme, PCAF, directly acetylates myosin in vitro, and actin has been implicated as a potential target of PCAF. Therefore, we attempted to acetylate actin with PCAF, in vitro, to determine its potential effect(s) on muscle function. PCAF underwent autoacetylation and bound to actin, yet failed to acetylate it. Chemical treatment of actin with acetic anhydride, however, increased lysine acetylation roughly 200-fold. Surprisingly, in vitro motility (IVM) of (100 μg/ml myosin concentration) and tropomyosin affinity for acetylated F-actin were indistinguishable from unacetylated control. However, IVM of acetylated F-actin, performed at low myosin concentration (12.5 μg/ml) and in the presence of tropomyosin, revealed a significant 63% increase in motile filaments relative to unacetylated control (p < 0.0001), suggesting that actin acetylation reduces tropomyosin-mediated inhibition of myosin binding. Since K326 and K328 have been reported as the most reactive lysines on actin, are acetylated in vivo, and pseudo-acetylation of both modulates muscle contraction, we assessed the effect of K326Q and K328Q pseudo-acetylated actin on Ca2+-mediated thin filament activation via regulated IVM. Although reconstituted thin filaments containing K326Q (pCa50 = 6.36 ± 0.03) did not alter Ca2+-sensitivity relative to WT (pCa50 = 6.37 ± 0.03), K328Q induced a significant leftward shift in Ca2+-sensitivity (ΔpCa50 = 0.19; p < 0.0001), consistent with a loss in tropomyosin-mediated inhibition. The data indicate that actin K328 acetylation modulates contractile function, which makes it a potential mechanism for regulating muscle performance in vivo." @default.
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- W2912279499 date "2019-02-01" @default.
- W2912279499 modified "2023-09-26" @default.
- W2912279499 title "Acetylation of Actin K328 Contributes to a Loss in Tropomyosin-Mediated Inhibition of Myosin Binding" @default.
- W2912279499 doi "https://doi.org/10.1016/j.bpj.2018.11.2467" @default.
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