A potential mechanism for regulating myosin I binding to membranes in vivo

FEBS Lett. 2000 Nov 3;484(2):125-8. doi: 10.1016/s0014-5793(00)02137-2.


Myosin Is are associated with specific membranes, however, the mechanism for regulating their intracellular localization is unclear. As a first step towards understanding this mechanism, membrane rebinding assays using Dictyostelium myoB were performed. Crude, cytosolic myoB bound to intact, but not to NaOH-treated plasma membranes. In contrast, partially purified myoB binds to both intact and NaOH-treated plasma membranes. Chemical cross-linking of cytosolic myoB yielded several products, whereas none were found with the partially purified myoB. These results suggest a model where proteins regulating the specific binding of myoB to the plasma membrane may exist both in the cytosol and on the plasma membrane.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cell Membrane / metabolism*
  • Cytosol / metabolism
  • Dictyostelium / cytology
  • Dictyostelium / metabolism*
  • Myosins / metabolism*
  • Protein Binding


  • Myosins