Tubulin subunit sorting: Analysis of the mechanisms involved in the segregation of unique tubulin isotypes within microtubule copolymers

D. B. Murphy

Research output: Contribution to journalArticle

Abstract

Vertebrate cells contain biochemical and genetic isotypes of tubulin which are expressed in unique combinations in different tissues and cell types. To determine if mixtures of tubulin isotypes assemble in vitro to form different classes of microtubules, we analyzed the composition of microtubule copolymers assembled from mixtures of chicken brain and erythrocyte tubulin. During microtubule elongation brain tubulin assembled onto the ends of microtubules faster than erythrocyte tubulin, resulting in copolymers with continually changing ratios of isotypes along their lengths. Unlike examples of microtubule assembly where the rate of polymerization depends on the association rate constant (k+) and the subunit concentration, the rate and extent of sorting in copolymers appear to depend on the dissociation rate constant (k-), which governs the rate at which subunits are released from tubulin oligomers and microtubules and thereby made available for reassembly into copolymers. The type of microtubule seed used to initiate elongation was also found to influence the composition of copolymers, indicating that polymerization favors association of subunits of the same isotype.

Original languageEnglish (US)
Pages (from-to)176-181
Number of pages6
JournalProtoplasma
Volume145
Issue number2-3
DOIs
Publication statusPublished - Jun 1988

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Keywords

  • Microtubules
  • Tubulin
  • Tubulin isotypes
  • Tubulin subunit sorting

ASJC Scopus subject areas

  • Cell Biology
  • Plant Science

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