Nock S, Liang W, Warrick H M, Spudich J A
Department of Biochemistry, Stanford University Medical Center, CA 94305-5307, USA.
FEBS Lett. 2000 Jan 28;466(2-3):267-72. doi: 10.1016/s0014-5793(99)01796-2.
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.
非肌肉肌球蛋白II丝的动态组装/拆卸对于酶活性的调节和定位至关重要。盘基网柄菌肌球蛋白II尾部的三个苏氨酸（1823、1833和2029）的磷酸化与肌球蛋白丝组装的控制有关。通过系统地将这三个苏氨酸替换为天冬氨酸，模拟磷酸化残基，我们发现1823位对于肌球蛋白丝形成和体内功能的调节最为关键。令人惊讶的是，单个电荷变化就能干扰肌球蛋白II的丝形成和体内功能。
