Proteomics

Dataset Information

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Lysine acetylation of F-actin decreases tropomyosin-based inhibition of actomyosin activity


ABSTRACT: Actin was acetylated on lysine residues with acetic anhydride to determine its impaction on the contractile properties of the thin filaments including, actin's ability to undergo crossbridge cycling with myosin, actin's affinity for tropomyosin, and the impact of actin acetylation on calcium regulated thin filament activation

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Oryctolagus Cuniculus (rabbit)

TISSUE(S): Skeletal Muscle

SUBMITTER: D. Brian Foster  

LAB HEAD: Brian Foster

PROVIDER: PXD020732 | Pride | 2020-09-04

REPOSITORIES: Pride

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Publications

Lysine acetylation of F-actin decreases tropomyosin-based inhibition of actomyosin activity.

Schmidt William W   Madan Aditi A   Foster D Brian DB   Cammarato Anthony A  

The Journal of biological chemistry 20200901 46


Recent proteomics studies of vertebrate striated muscle have identified lysine acetylation at several sites on actin. Acetylation is a reversible post-translational modification that neutralizes lysine's positive charge. Positively charged residues on actin, particularly Lys<sup>326</sup> and Lys<sup>328</sup>, are predicted to form critical electrostatic interactions with tropomyosin (Tpm) that promote its binding to filamentous (F)-actin and bias Tpm to an azimuthal location where it impedes m  ...[more]

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