Isolation of actin-binding protein and villin from toad oocytes

Developmental Biology
H L Corwin, J H Hartwig

Abstract

Two actin-modulating proteins have been purified from toad oocytes. A high-molecular weight protein, similar in structure and function to macrophage actin-binding protein, accounts for the isotropic actin-crosslinking activity in oocyte homogenates. A calcium-dependent activity in toad oocyte homogenates which shortens actin filaments is accounted for by a 95,000-dalton protein which resembles villin, an actin-severing and -bundling protein of avian epithelial brush borders. In the presence of high (greater than or equal to microM) calcium, this protein shortens actin filaments in a concentration-dependent fashion and stimulates filament assembly when added to monomeric actin. In the absence of calcium the protein promotes the formation of actin filament bundles. Therefore, in the toad oocyte actin can be crosslinked into a network by actin-binding protein. Calcium regulation of the actin network may be mediated by villin. These results are different from those reported in echinoderm eggs.

References

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Citations

Mar 1, 1992·Cancer Metastasis Reviews·C C Cunningham
Nov 1, 1989·Cell Differentiation and Development : the Official Journal of the International Society of Developmental Biologists·M Charbonneau, N Grandin
Sep 1, 1990·The Journal of Cell Biology·J B GorlinJ H Hartwig
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Jan 1, 1987·Cell Motility and the Cytoskeleton·S Yonemura, I Mabuchi
Nov 1, 1987·The American Journal of Physiology·J H HartwigD Brown

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