Expression of amino- and carboxyl-terminal gamma- and alpha-tubulin mutants in cultured epithelial cells.

The Journal of Biological Chemistry
A Leask, T Stearns

Abstract

Three distinct tubulin proteins are essential for microtubule function: alpha-, beta-, and gamma-tubulin. After translation, alpha- and beta-tubulin proteins combine into a soluble, 7 S heterodimer that is multimerized to form the microtubule filament. Conversely, gamma-tubulin combines with several proteins into a soluble, 25 S multi-protein particle, the gammasome that is essential for nucleating microtubule filaments at the centrosome. The proteins that assist tubulins in executing their specific functions are largely unknown. As an initial approach to address this issue, we first decided to identify domains of mammalian alpha- and gamma-tubulin necessary for their function by creating mutant mammalian alpha- and gamma-tubulin (both deletion and hybrid mutants) and assaying their behavior in stably transfected Chinese hamster ovary epithelial cells. First, we demonstrated that addition of a carboxyl-terminal epitope tag had no effect on the subcellular localization of either alpha- and gamma-tubulin. Second, we found that both the amino and carboxyl termini of gamma-tubulin were essential for its incorporation into the gammasome. Third, we found that the amino and carboxyl termini of alpha-tubulin were necessary for incorpor...Continue Reading

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Citations

Mar 11, 2000·Molecular Cell·C DongP J Goldschmidt-Clermont
Feb 3, 1999·Annual Review of Genetics·J W Jarvik, C A Telmer
Dec 10, 2002·Annual Review of Pharmacology and Toxicology·Kim BoekelheideStephanie Thompson
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Jul 10, 2001·Annual Review of Biophysics and Biomolecular Structure·E Nogales
Apr 12, 2005·The Biochemical Journal·Tomoya Kotani, Masakane Yamashita
May 23, 2002·European Journal of Cell Biology·Christine Daunderer, Ralph O Gräf

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