Microtubule stabilization in vivo by nucleation-incompetent γ-tubulin complex

Autor: Kenneth E. Sawin, Andreas Anders
Jazyk: angličtina
Rok vydání: 2011
Předmět:
Zdroj: Journal of Cell Science
Anders, A & Sawin, K E 2011, ' Microtubule stabilization in vivo by nucleation-incompetent gamma-tubulin complex ', Journal of Cell Science, vol. 124, no. 8, pp. 1207-1213 . https://doi.org/10.1242/jcs.083741
ISSN: 1477-9137
0021-9533
DOI: 10.1242/jcs.083741
Popis: Although the fission yeast Schizosaccharomyces pombe contains many of the gamma-tubulin ring complex (gamma-TuRC)-specific proteins of the gamma-tubulin complex (gamma-TuC), several questions about the organizational state and function of the fission yeast gamma-TuC in vivo remain unresolved. Using 3 x GFP-tagged gamma-TuRC-specific proteins, we show here that gamma-TuRC-specific proteins are present at all microtubule organizing centers in fission yeast and that association of gamma-TuRC-specific proteins with the gamma-tubulin small complex (gamma-TuSC) does not depend on Mto1, which is a key regulator of the gamma-TuC. Through sensitive imaging in mto1 Delta mutants, in which cytoplasmic microtubule nucleation is abolished, we unexpectedly found that gamma-TuC incapable of nucleating microtubules can nevertheless associate with microtubule minus-ends in vivo. The presence of gamma-TuC at microtubule ends is independent of gamma-TuRC-specific proteins and strongly correlates with the stability of microtubule ends. Strikingly, microtubule bundles lacking gamma-TuC at microtubule ends undergo extensive treadmilling in vivo, apparently induced by geometrical constraints on plus-end growth. Our results indicate that microtubule stabilization by the gamma-TuC, independently of its nucleation function, is important for maintaining the organization and dynamic behavior of microtubule arrays in vivo.
Databáze: OpenAIRE