Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors
Abstract The γ-tubulin ring complex (γ-TuRC) is a structural template for controlled nucleation of microtubules from α/β-tubulin heterodimers. At the cytoplasmic side of the yeast spindle pole body, the CM1-containing receptor protein Spc72 promotes γ-TuRC assembly from seven γ-tubulin small complex...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2025-01-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-024-55778-7 |
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| _version_ | 1841544498803376128 |
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| author | Anjun Zheng Bram J. A. Vermeulen Martin Würtz Annett Neuner Nicole Lübbehusen Matthias P. Mayer Elmar Schiebel Stefan Pfeffer |
| author_facet | Anjun Zheng Bram J. A. Vermeulen Martin Würtz Annett Neuner Nicole Lübbehusen Matthias P. Mayer Elmar Schiebel Stefan Pfeffer |
| author_sort | Anjun Zheng |
| collection | DOAJ |
| description | Abstract The γ-tubulin ring complex (γ-TuRC) is a structural template for controlled nucleation of microtubules from α/β-tubulin heterodimers. At the cytoplasmic side of the yeast spindle pole body, the CM1-containing receptor protein Spc72 promotes γ-TuRC assembly from seven γ-tubulin small complexes (γ-TuSCs) and recruits the microtubule polymerase Stu2, yet their molecular interplay remains unclear. Here, we determine the cryo-EM structure of the Candida albicans cytoplasmic nucleation unit at 3.6 Å resolution, revealing how the γ-TuRC is assembled and conformationally primed for microtubule nucleation by the dimerised Spc72 CM1 motif. Two coiled-coil regions of Spc72 interact with the conserved C-terminal α-helix of Stu2 and thereby position the α/β-tubulin-binding TOG domains of Stu2 in the vicinity of the microtubule assembly site. Collectively, we reveal the function of CM1 motifs in γ-TuSC oligomerisation and the recruitment of microtubule polymerases to the γ-TuRC. |
| format | Article |
| id | doaj-art-3035899de3af45778b2c1d6dcea0d2b9 |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-3035899de3af45778b2c1d6dcea0d2b92025-01-12T12:29:40ZengNature PortfolioNature Communications2041-17232025-01-0116111910.1038/s41467-024-55778-7Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptorsAnjun Zheng0Bram J. A. Vermeulen1Martin Würtz2Annett Neuner3Nicole Lübbehusen4Matthias P. Mayer5Elmar Schiebel6Stefan Pfeffer7Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)Abstract The γ-tubulin ring complex (γ-TuRC) is a structural template for controlled nucleation of microtubules from α/β-tubulin heterodimers. At the cytoplasmic side of the yeast spindle pole body, the CM1-containing receptor protein Spc72 promotes γ-TuRC assembly from seven γ-tubulin small complexes (γ-TuSCs) and recruits the microtubule polymerase Stu2, yet their molecular interplay remains unclear. Here, we determine the cryo-EM structure of the Candida albicans cytoplasmic nucleation unit at 3.6 Å resolution, revealing how the γ-TuRC is assembled and conformationally primed for microtubule nucleation by the dimerised Spc72 CM1 motif. Two coiled-coil regions of Spc72 interact with the conserved C-terminal α-helix of Stu2 and thereby position the α/β-tubulin-binding TOG domains of Stu2 in the vicinity of the microtubule assembly site. Collectively, we reveal the function of CM1 motifs in γ-TuSC oligomerisation and the recruitment of microtubule polymerases to the γ-TuRC.https://doi.org/10.1038/s41467-024-55778-7 |
| spellingShingle | Anjun Zheng Bram J. A. Vermeulen Martin Würtz Annett Neuner Nicole Lübbehusen Matthias P. Mayer Elmar Schiebel Stefan Pfeffer Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors Nature Communications |
| title | Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors |
| title_full | Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors |
| title_fullStr | Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors |
| title_full_unstemmed | Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors |
| title_short | Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors |
| title_sort | structural insights into the interplay between microtubule polymerases γ tubulin complexes and their receptors |
| url | https://doi.org/10.1038/s41467-024-55778-7 |
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