Class I myosins are single-headed motor proteins, implicated in various motile processes including organelle translocation, ion-channel gating, and cytoskeleton reorganization. Here we describe the cellular localization of myosin-IE and its role in the phagocytic uptake of solid particles and cells. A complete analysis of the kinetic and motor properties of Dictyostelium discoideum myosin-IE was achieved by the use of motor domain constructs with artificial lever arms. Class I myosins belonging to subclass IC like myosin-IE are thought to be tuned for tension maintenance or stress sensing. In contrast to this prediction, our results show myosin-IE to be a fast motor. Myosin-IE motor activity is regulated by myosin heavy chain phosphorylation, which increases the coupling efficiency betw n the actin and nucleotide binding sites tenfold and the motile activity more than fivefold. Changes in the level of free Mg2+ ions, which are within the physiological range, are shown to modulate the motor activity of myosin-IE by inhibiting the release of adenosine diphosphate.
Dürrwang, U., Fujita-Becker, S., Erent, M., Kull, F. J., Tsiavaliaris, G., Geeves, M. A., & Manstein, D. J. (2006). Dictyostelium myosin-IE is a fast molecular motor involved in phagocytosis. Journal of Cell Science, 119(3), 550–558. https://doi.org/10.1242/jcs.02774