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Actin pp 205-213 | Cite as

Brush Border Myosin I Has A Calmodulin/Phosphatidylserine Switch and Tail Actin-Binding

  • Helena Swanljung-Collins
  • Jimmy H. Collins
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 358)

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.

Keywords

ATPase Activity Heavy Chain Soluble Class Cell BioI Effect ofCa2 
These 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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Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Helena Swanljung-Collins
    • 1
  • Jimmy H. Collins
    • 1
  1. 1.Department of BiochemistryTemple University School of MedicinePhiladelphiaUSA

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