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. Copyright (C) 2000 Federation of European Biochemical Societies.
|Original language||English (US)|
|Number of pages||4|
|State||Published - Nov 3 2000|
Bibliographical noteFunding Information:
The authors would like to thank Drs. Dan Kiehart, Mike Sheetz, Pat Casey, and Vann Bennett for valuable discussions during the course of this study. We would also like to thank Dr. Joe Kelleher for helpful comments on the manuscript. This work was supported by NIH grant GM-46486 to M.A.T.
- Dictyostelium discoideum
- Membrane association
- Myosin I
- Plasma membrane
- Unconventional myosin