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Reference: Erlemann S, et al. (2012) An extended gamma-tubulin ring functions as a stable platform in microtubule nucleation. J Cell Biol 197(1):59-74

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Abstract


gamma-Tubulin complexes are essential for microtubule (MT) nucleation. The gamma-tubulin small complex (gamma-TuSC) consists of two molecules of gamma-tubulin and one molecule each of Spc97 and Spc98. In vitro, gamma-TuSCs oligomerize into spirals of 13 gamma-tubulin molecules per turn. However, the properties and numbers of gamma-TuSCs at MT nucleation sites in vivo are unclear. In this paper, we show by fluorescence recovery after photobleaching analysis that gamma-tubulin was stably integrated into MT nucleation sites and was further stabilized by tubulin binding. Importantly, tubulin showed a stronger interaction with the nucleation site than with the MT plus end, which probably provides the basis for MT nucleation. Quantitative analysis of gamma-TuSCs on single MT minus ends argued for nucleation sites consisting of approximately seven gamma-TuSCs with approximately three additional gamma-tubulin molecules. Nucleation and anchoring of MTs required the same number of gamma-tubulin molecules. We suggest that a spiral of seven gamma-TuSCs with a slight surplus of gamma-tubulin nucleates MTs in vivo.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Erlemann S, Neuner A, Gombos L, Gibeaux R, Antony C, Schiebel E
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