GTP regulates the microtubule nucleation activity of γ-tubulin
Both subunits of αβ-tubulin that comprise the core components of microtubules bind GTP. GTP binding to α-tubulin has a structural role, whereas β-tubulin binds and hydrolyses GTP to regulate microtubule dynamics. γ-tubulin, another member of the tubulin superfamily that seeds microtubule nucleation...
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| Main Authors: | , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
27 October 2013
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| In: |
Nature cell biology
Year: 2013, Volume: 15, Issue: 11, Pages: 1317-1327 |
| ISSN: | 1476-4679 |
| DOI: | 10.1038/ncb2863 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/ncb2863 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/ncb2863 
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| Author Notes: | Linda Gombos, Annett Neuner, Mykhaylo Berynskyy, Luca L. Fava, Rebecca C. Wade, Carsten Sachse and Elmar Schiebel |
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| 520 | |a Both subunits of αβ-tubulin that comprise the core components of microtubules bind GTP. GTP binding to α-tubulin has a structural role, whereas β-tubulin binds and hydrolyses GTP to regulate microtubule dynamics. γ-tubulin, another member of the tubulin superfamily that seeds microtubule nucleation at microtubule-organizing centres, also binds GTP; however, the importance of this association remains elusive. To address the role of GTP binding to γ-tubulin, we systematically mutagenized the GTP contact residues in the yeast γ-tubulin Tub4. Tub4GTP-mutant proteins that exhibited greatly reduced GTP affinity still assembled into the small γ-tubulin complex. However, tub4GTP mutants were no longer viable, and had defects in interaction between γ-tubulin and αβ-tubulin, decreased microtubule nucleation and defects in microtubule organization. In vitro and in vivo data show that only γ-tubulin loaded with GTP nucleates microtubules. Our results suggest that GTP recruitment to γ-tubulin enhances its interaction with αβ-tubulin similarly to GTP recruitment to β-tubulin. | ||
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