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Journal of Cell Science, Vol 79, Issue 1 199-215, Copyright © 1985 by Company of Biologists

JOURNAL ARTICLES

Xenopus marginal band disassembly by calcium-activated cytoplasmic factors

J Gambino, MJ Ross, JA Weatherbee, RH Gavin and RA Eckhardt

The marginal band microtubules of isolated Xenopus erythrocyte cytoskeletons possess the stability properties of non-steady-state microtubules. They are unperturbed by low temperatures, a variety of microtubule inhibitors, hypotonic treatment and the direct action of calcium. These microtubules can be rapidly depolymerized by erythrocyte lysis in the presence of calcium or by exposure of cytoskeletons obtained and washed in calcium-free media to calcium-containing supernatants of other cell lysates. Thus, marginal band microtubules are calcium-sensitive only in the presence of cytoplasm. The calcium-activated disassembly of the marginal band does not appear to be the result of general or tubulin-specific proteolysis and is prevented by the calmodulin inhibitor, trifluoperazine. On sodium dodecyl sulphate/polyacrylamide gels, samples of calcium-induced, marginal band disassembled cytoskeletons are always tubulin-depleted and also possess a new high molecular weight polypeptide doublet that is believed to constitute stable partial degradation products of spectrin. In the presence of calcium, addition of calmodulin and ATP to cytoskeletons washed free of cytoplasm does not initiate marginal band disassembly. Therefore, if calmodulin mediates marginal band disassembly, it requires cytoplasmic binding proteins or cytoplasmic cofactors.


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J Zhu, S. Bloom, E Lazarides, and C Woods
Identification of a novel Ca(2+)-regulated protein that is associated with the marginal band and centrosomes of chicken erythrocytes
J. Cell Sci., January 2, 1995; 108(2): 685 - 698.
[Abstract] [PDF]


© The Company of Biologists Ltd 1985