Erythrocyte microtubule assembly in vitro. Tubulin oligomers limit the rate of microtubule self-assembly

D. B. Murphy, K. T. Wallis

Research output: Contribution to journalArticlepeer-review

Abstract

Chicken erythrocyte tubulin containing a unique β tubulin variant polymerizes with greater efficiency (lower critical concentration) but at a slower rate than chicken brain tubulin. In a previous study we demonstrated that the low net rate of assembly is partly due to the presence of large oligomers and rings which reduce the initial rate of subunit elongation on microtubule seeds (Murphy, D.B., and Wallis, K.T. (1985) J. Biol. Chem. 260, 12293-12301). In this study we show that erythrocyte tubulin oligomers also retard the rate of microtubule nucleation and the net rate of self-assembly. The inhibitory effect is most likely to be due to the increased stability of erythrocyte tubulin oligomers, including a novel polymer of coiled rings that forms during the rapid phase of microtubule polymerization. The slow rate of dissociation of rings and coils into dimers and small oligomers appears to limit both the nucleation and elongation steps in the self-assembly of erythrocyte microtubules.

Original languageEnglish (US)
Pages (from-to)2319-2324
Number of pages6
JournalJournal of Biological Chemistry
Volume261
Issue number5
StatePublished - 1986

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Erythrocyte microtubule assembly in vitro. Tubulin oligomers limit the rate of microtubule self-assembly'. Together they form a unique fingerprint.

Cite this