Microtubule protein preparations from C6 glial cells and their spontaneous polymer formation.
Year: 1979
Type: article
Abstract: C6 cell tubulin is indistinguishable from hog brain tubulin with respect to its molecular weight, amino acid composition, and colchicine-binding activity. Moreover, microtubule assembly systems from both sources form the same structures: rings, ribbons, tubules, and drug-induced polymers. There is, nevertheless, a difference between the cultured cell and brain systems which lies in the nature of their microtubule-associated accessory proteins. C6 microtubule preparations exhibit few rings at 0 degrees C, have low polymerization yield, and have a low content of accessory proteins. The addition of brain accessory proteins enhances the numbers of rings, and the yield of microtubules, to levels comparable with those of brain preparations. The polymerizing ability of C6 microtubule protein decays much faster than that of brain, but it can be restored by the addition of brain accessory protein. The results suggest that C6 accessory proteins are more labile than their brain counterparts.
Source: The Journal of Cell Biology
DOI: 10.1083/jcb.80.3.553
Authors: G Wiche, L S Honig, R D Cole
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2170085018