Abstract
Brush border myosin I (BBMI) interacts with the actin filaments bundled in the structural core of microvilli in intestinal epithelial cells and links the filaments to the microvillar plasma membrane. This highly organized system may provide insights into how actin interacts with cell membranes via the myosin I class of motor proteins. In this paper we present studies of the mechanism and regulation by Ca2+ of myosin I binding to the membrane lipid phosphatidylserine (PS), studies of Ca2+ regulation of the myosin I ATPase activity, and studies of the apparent interaction of BBMI with actin through a site in the COOH-terminal domain of BBMI.KeywordsATPase ActivityHeavy ChainSoluble ClassCell BioIEffect ofCa2These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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