Phosphorylation of Ser283 enhances the stiffness of the tropomyosin head-to-tail overlap domain

Archives of Biochemistry and Biophysics
William LehmanMichael Regnier

Abstract

The ends of coiled-coil tropomyosin molecules are joined together by nine to ten residue-long head-to-tail "overlapping domains". These short four-chained interconnections ensure formation of continuous tropomyosin cables that wrap around actin filaments. Molecular Dynamics simulations indicate that the curvature and bending flexibility at the overlap is 10-20% greater than over the rest of the molecule, which might affect head-to-tail filament assembly on F-actin. Since the penultimate residue of striated muscle tropomyosin, Ser283, is a natural target of phosphorylating enzymes, we have assessed here if phosphorylation adjusts the mechanical properties of the tropomyosin overlap domain. MD simulations show that phosphorylation straightens the overlap to match the curvature of the remainder of tropomyosin while stiffening it to equal or exceed the rigidity of canonical coiled-coil regions. Corresponding EM data on phosphomimetic tropomyosin S283D corroborate these findings. The phosphorylation-induced change in mechanical properties of tropomyosin likely results from electrostatic interactions between C-terminal phosphoSer283 and N-terminal Lys12 in the four-chain overlap bundle, while promoting stronger interactions among sur...Continue Reading

Citations

Feb 20, 2016·Archives of Biochemistry and Biophysics·Jeffrey R MooreWilliam Lehman
Sep 20, 2019·Journal of Muscle Research and Cell Motility·Galina V KopylovaAndrey K Tsaturyan
Oct 4, 2018·Scientific Reports·Jacopo SgrignaniAndrea Cavalli
Jan 4, 2021·Journal of Muscle Research and Cell Motility·Galina V KopylovaDaniil V Shchepkin
Sep 25, 2019·Biophysical Journal·Yasser AboelkassemAndrew D McCulloch
Nov 2, 2020·International Journal of Biological Macromolecules·Victoria V NefedovaDmitrii I Levitsky
Mar 6, 2019·Journal of the American Society for Mass Spectrometry·Yutong JinYing Ge

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