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
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 358)


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.


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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    H. Swanljung-Collins and J.H. Collins, Ca2+ stimulates the Mg2+-ATPase activity of brush border myosin I with three or four calmodulin light chains but inhibits with less than two bound., J. Biol. Chem. 266: 1312 (1991).PubMedGoogle Scholar
  2. 2.
    K. Collins, J.R. Sellers, and P. Matsudaira, Calmodulin dissociation regulates brush border myosin-I (110K-calmodulin) activity in vitro, J.Cell Biol. 110: 1137 (1990).PubMedCrossRefGoogle Scholar
  3. 3.
    L.M. Coluccio and A. Bretscher, Calcium-regulated cooperative binding of the microvillar 110K-calmodulin complex to F-actin, J. Cell Biol. 105: 325 (1987).PubMedCrossRefGoogle Scholar
  4. 4.
    H. Swanljung-Collins and J.H. Collins, Phosphorylation of brush border myosin I by protein kinase C is regulated by Ca2+-stimulated binding of myosin I to phosphatidylserine concerted with calmodulin dissociation, J. Biol. Chem. 267: 3445 (1992).PubMedGoogle Scholar
  5. 5.
    K.A. Alexander, B. Cimler, K.E. Meier, and D.R. Storm, Regulation of calmodulin binding to P-57, J. Biol. Chem. 262: 6108 (1987).PubMedGoogle Scholar
  6. 6.
    S.M. Hayden, J.S. Wolenski, and M.S. Mooseker, Binding of myosin I to phospholipid vesicles, J. Cell Biol. 111: 443 (1990).PubMedCrossRefGoogle Scholar
  7. 7.
    A. Garcian, E. Coudrier, J. Carboni, J. Anderson, J. Vandekerkhove, M. Mooseker, D. Louvard, and M. Arpin, Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin-I family, J. Cell Biol. 109: 2895 (1989).CrossRefGoogle Scholar
  8. 8.
    E.R. Chapman, D. Au, K.A. Alexander, T.A. Nicolson, and D.R. Storm, Characterization of the calmodulin binding domain of neuromodulin: functional significance of serine 41 and phenylalanine 42, J. Biol. Chem. 266: 207 (1991).PubMedGoogle Scholar
  9. 9.
    J. Baudier, J.C. Deloulme, A. Van Dorsselaer, D. Black, and H.W.D. Matthes, Purification and characterization of a brain-specific protein kinase C substrate, neurogranin (p17). Identificaiton of a consensus amino acid sequence between neurogranins and neuromodulin (GAP43) that correspond to the protein kinase C phosphorylation site and the calmodulin-binding domain, J. Biol. Chem. 266: 229 (1991).PubMedGoogle Scholar
  10. 10.
    D.J. Halsall and J.A. Hammer, A second isoform of chicken brush border myosin I contains a 29-residue inserted sequence that binds calmodulin, FEBS Lett. 267: 1: 126 (1990).PubMedCrossRefGoogle Scholar
  11. 11.
    M. Hoshimaru, Y. Fujio, K. Sobue, T. Sugimoto, and S. Nakanishi, Immunochemical evidence that myosin I heavy chain-like protein is identical to the 110-kilodalton brush-border protein, J. Biochem. 106: 455 (1989).PubMedGoogle Scholar
  12. 12.
    L. Nyitray, E.B. Goodwin, and A.G. Szent-Gyorgy, Complete primary structure of a scallop striated muscle myosin heavy chain: sequence comparison with other heavy chains reveals regions that might be critical for regulation, J. Biol. Chem. 266: 18469 (1991).PubMedGoogle Scholar
  13. 13.
    J.A. Mercer, P.K. Seperack, M.C. Strobel, N. Copeland G., and N.A. Jenkins, Novel myosin heavy chain encoded by murine dilute coat colour locus, Nature 349: 709 (1991).PubMedCrossRefGoogle Scholar
  14. 14.
    E.D. Korn and J.A. Hammer 3d, Myosin I, Curr. Opinion Cell Biol. 2: 57 (1990).PubMedCrossRefGoogle Scholar

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

Personalised recommendations