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Mutational analysis of phosphorylation sites in theDictyosteliummyosin II tail: disruption of myosin function by a single charge change

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
466
Identifiers
DOI: 10.1016/s0014-5793(99)01796-2
Keywords
  • Myosin
  • Phosphorylation
  • Filament Formation

Abstract

Abstract The dynamic assembly/disassembly of non-muscle myosin II filaments is critical for the regulation of enzymatic activities and localization. Phosphorylation of three threonines, 1823, 1833 and 2029, in the tail of Dictyostelium discoideum myosin II has been implicated in control of myosin filament assembly. By systematically replacing the three threonines to aspartates, mimicking a phosphorylated residue, we found that position 1823 is the most critical one for the regulation of myosin filament formation and in vivo function. Surprisingly, a single charge change is able to perturb filament formation and in vivo function of myosin II.

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