학술논문
Mutational analysis of phosphorylation sites in the Dictyosteliummyosin II tail: disruption of myosin function by a single charge change
Document Type
Article
Source
FEBS Letters; January 2000, Vol. 466 Issue: 2-3 p267-272, 6p
Subject
Language
ISSN
00145793
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 discoideummyosin 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.