{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T01:51:05Z","timestamp":1787881865912,"version":"build-2784847793"},"reference-count":80,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2025,1,5]],"date-time":"2025-01-05T00:00:00Z","timestamp":1736035200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2025,1,5]],"date-time":"2025-01-05T00:00:00Z","timestamp":1736035200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["PF 963\/4-1"],"award-info":[{"award-number":["PF 963\/4-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["PF 963\/1-4"],"award-info":[{"award-number":["PF 963\/1-4"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["Schi 295\/4-4"],"award-info":[{"award-number":["Schi 295\/4-4"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Commun"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    The \u03b3-tubulin ring complex (\u03b3-TuRC) is a structural template for controlled nucleation of microtubules from \u03b1\/\u03b2-tubulin heterodimers. At the cytoplasmic side of the yeast spindle pole body, the CM1-containing receptor protein Spc72 promotes \u03b3-TuRC assembly from seven \u03b3-tubulin small complexes (\u03b3-TuSCs) and recruits the microtubule polymerase Stu2, yet their molecular interplay remains unclear. Here, we determine the cryo-EM structure of the\n                    <jats:italic>Candida albicans<\/jats:italic>\n                    cytoplasmic nucleation unit at 3.6\u2009\u00c5 resolution, revealing how the \u03b3-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 \u03b1-helix of Stu2 and thereby position the \u03b1\/\u03b2-tubulin-binding TOG domains of Stu2 in the vicinity of the microtubule assembly site. Collectively, we reveal the function of CM1 motifs in \u03b3-TuSC oligomerisation and the recruitment of microtubule polymerases to the \u03b3-TuRC.\n                  <\/jats:p>","DOI":"10.1038\/s41467-024-55778-7","type":"journal-article","created":{"date-parts":[[2025,1,5]],"date-time":"2025-01-05T08:03:28Z","timestamp":1736064208000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Structural insights into the interplay between microtubule polymerases, \u03b3-tubulin complexes and their receptors"],"prefix":"10.1038","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0009-0008-4922-6509","authenticated-orcid":false,"given":"Anjun","family":"Zheng","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9798-6245","authenticated-orcid":false,"given":"Bram J. A.","family":"Vermeulen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4504-4723","authenticated-orcid":false,"given":"Martin","family":"W\u00fcrtz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Annett","family":"Neuner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-2200-5904","authenticated-orcid":false,"given":"Nicole","family":"L\u00fcbbehusen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7859-3112","authenticated-orcid":false,"given":"Matthias P.","family":"Mayer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3683-247X","authenticated-orcid":false,"given":"Elmar","family":"Schiebel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5843-2795","authenticated-orcid":false,"given":"Stefan","family":"Pfeffer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,1,5]]},"reference":[{"key":"55778_CR1","doi-asserted-by":"publisher","first-page":"a022608","DOI":"10.1101\/cshperspect.a022608","volume":"10","author":"HV Goodson","year":"2018","unstructured":"Goodson, H. V. & Jonasson, E. M. Microtubules and microtubule-associated proteins. Cold Spring Harb. Perspect. Biol. 10, a022608 (2018).","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"55778_CR2","doi-asserted-by":"publisher","first-page":"1187","DOI":"10.1007\/s00709-016-1070-z","volume":"254","author":"V Sulimenko","year":"2017","unstructured":"Sulimenko, V., Hajkova, Z., Klebanovych, A. & Draber, P. Regulation of microtubule nucleation mediated by gamma-tubulin complexes. Protoplasma 254, 1187\u20131199 (2017).","journal-title":"Protoplasma"},{"key":"55778_CR3","first-page":"4445","volume":"125","author":"N Teixido-Travesa","year":"2012","unstructured":"Teixido-Travesa, N., Roig, J. & Luders, J. The where, when and how of microtubule nucleation - one ring to rule them all. J. Cell Sci. 125, 4445\u20134456 (2012).","journal-title":"J. Cell Sci."},{"key":"55778_CR4","doi-asserted-by":"publisher","first-page":"765","DOI":"10.1042\/EBC20180028","volume":"62","author":"CA Tovey","year":"2018","unstructured":"Tovey, C. A. & Conduit, P. T. Microtubule nucleation by gamma-tubulin complexes and beyond. Essays Biochem 62, 765\u2013780 (2018).","journal-title":"Essays Biochem"},{"key":"55778_CR5","doi-asserted-by":"publisher","first-page":"467","DOI":"10.1038\/s41586-019-1896-6","volume":"578","author":"P Liu","year":"2020","unstructured":"Liu, P. et al. Insights into the assembly and activation of the microtubule nucleator gamma-TuRC. Nature 578, 467\u2013471 (2020).","journal-title":"Nature"},{"key":"55778_CR6","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1016\/j.cell.2019.12.007","volume":"180","author":"M Wieczorek","year":"2020","unstructured":"Wieczorek, M. et al. Asymmetric molecular architecture of the human gamma-tubulin ring complex. Cell 180, 165\u2013175.e116 (2020).","journal-title":"Cell"},{"key":"55778_CR7","doi-asserted-by":"publisher","first-page":"603","DOI":"10.1016\/j.devcel.2020.04.019","volume":"53","author":"T Consolati","year":"2020","unstructured":"Consolati, T. et al. Microtubule nucleation properties of single human gammaturcs explained by their cryo-EM structure. Dev. Cell 53, 603\u2013617.e608 (2020).","journal-title":"Dev. Cell"},{"key":"55778_CR8","doi-asserted-by":"publisher","first-page":"5075","DOI":"10.1091\/mbc.e05-11-1009","volume":"17","author":"A Anders","year":"2006","unstructured":"Anders, A., Lourenco, P. C. & Sawin, K. E. Noncore components of the fission yeast gamma-tubulin complex. Mol. Biol. Cell 17, 5075\u20135093 (2006).","journal-title":"Mol. Biol. Cell"},{"key":"55778_CR9","doi-asserted-by":"publisher","first-page":"4218","DOI":"10.1242\/jcs.059196","volume":"122","author":"Y Xiong","year":"2009","unstructured":"Xiong, Y. & Oakley, B. R. In vivo analysis of the functions of gamma-tubulin-complex proteins. J. Cell Sci. 122, 4218\u20134227 (2009).","journal-title":"J. Cell Sci."},{"key":"55778_CR10","doi-asserted-by":"publisher","first-page":"e65168","DOI":"10.7554\/eLife.65168","volume":"10","author":"AF Brilot","year":"2021","unstructured":"Brilot, A. F. et al. CM1-driven assembly and activation of yeast gamma-tubulin small complex underlies microtubule nucleation. Elife 10, e65168 (2021).","journal-title":"Elife"},{"key":"55778_CR11","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-020-19456-8","volume":"11","author":"E Zupa","year":"2020","unstructured":"Zupa, E. et al. The cryo-EM structure of a gamma-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems. Nat. Commun. 11, 5705 (2020).","journal-title":"Nat. Commun."},{"key":"55778_CR12","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/0047-7206(82)90078-4","volume":"13","author":"SM King","year":"1982","unstructured":"King, S. M. & Hyams, J. S. The mitotic spindle of Saccharomyces cerevisiae: assembly, structure and function. Micron (1969) 13, 93\u2013117 (1982).","journal-title":"Micron (1969)"},{"key":"55778_CR13","doi-asserted-by":"publisher","first-page":"132","DOI":"10.1038\/nsmb.2953","volume":"22","author":"JM Kollman","year":"2015","unstructured":"Kollman, J. M. et al. Ring closure activates yeast gammaTuRC for species-specific microtubule nucleation. Nat. Struct. Mol. Biol. 22, 132\u2013137 (2015).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"55778_CR14","doi-asserted-by":"publisher","first-page":"879","DOI":"10.1038\/nature09207","volume":"466","author":"JM Kollman","year":"2010","unstructured":"Kollman, J. M., Polka, J. K., Zelter, A., Davis, T. N. & Agard, D. A. Microtubule nucleating gamma-TuSC assembles structures with 13-fold microtubule-like symmetry. Nature 466, 879\u2013882 (2010).","journal-title":"Nature"},{"key":"55778_CR15","doi-asserted-by":"crossref","unstructured":"Dendooven, T. et al. Structure of the native gamma-tubulin ring complex capping spindle microtubules. Nat. Struct. Mol. Biol. 31, 1134\u20131144(2024).","DOI":"10.1038\/s41594-024-01281-y"},{"key":"55778_CR16","doi-asserted-by":"publisher","first-page":"4037","DOI":"10.1091\/mbc.e07-05-0474","volume":"18","author":"J Zhang","year":"2007","unstructured":"Zhang, J. & Megraw, T. L. Proper recruitment of gamma-tubulin and D-TACC\/Msps to embryonic Drosophila centrosomes requires Centrosomin Motif 1. Mol. Biol. Cell 18, 4037\u20134049 (2007).","journal-title":"Mol. Biol. Cell"},{"key":"55778_CR17","doi-asserted-by":"publisher","first-page":"e80053","DOI":"10.7554\/eLife.80053","volume":"11","author":"MJ Rale","year":"2022","unstructured":"Rale, M. J., Romer, B., Mahon, B. P., Travis, S. M. & Petry, S. The conserved centrosomin motif, gammaTuNA, forms a dimer that directly activates microtubule nucleation by the gamma-tubulin ring complex (gammaTuRC). Elife 11, e80053 (2022).","journal-title":"Elife"},{"key":"55778_CR18","doi-asserted-by":"publisher","first-page":"1089","DOI":"10.1083\/jcb.201007030","volume":"191","author":"YK Choi","year":"2010","unstructured":"Choi, Y. K., Liu, P., Sze, S. K., Dai, C. & Qi, R. Z. CDK5RAP2 stimulates microtubule nucleation by the gamma-tubulin ring complex. J. Cell Biol. 191, 1089\u20131095 (2010).","journal-title":"J. Cell Biol."},{"key":"55778_CR19","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1083\/jcb.201601099","volume":"213","author":"A Muroyama","year":"2016","unstructured":"Muroyama, A., Seldin, L. & Lechler, T. Divergent regulation of functionally distinct gamma-tubulin complexes during differentiation. J. Cell Biol. 213, 679\u2013692 (2016).","journal-title":"J. Cell Biol."},{"key":"55778_CR20","doi-asserted-by":"publisher","first-page":"823","DOI":"10.1083\/jcb.201606092","volume":"215","author":"TC Lin","year":"2016","unstructured":"Lin, T. C. et al. MOZART1 and gamma-tubulin complex receptors are both required to turn gamma-TuSC into an active microtubule nucleation template. J. Cell Biol. 215, 823\u2013840 (2016).","journal-title":"J. Cell Biol."},{"key":"55778_CR21","doi-asserted-by":"publisher","first-page":"107791","DOI":"10.1016\/j.celrep.2020.107791","volume":"31","author":"M Wieczorek","year":"2020","unstructured":"Wieczorek, M., Huang, T. L., Urnavicius, L., Hsia, K. C. & Kapoor, T. M. MZT Proteins Form Multi-Faceted Structural Modules in the gamma-Tubulin Ring Complex. Cell Rep. 31, 107791 (2020).","journal-title":"Cell Rep."},{"key":"55778_CR22","doi-asserted-by":"publisher","unstructured":"Xu, Y. et al. Partial closure of the gamma-tubulin ring complex by CDK5RAP2 activates microtubule nucleation. Dev Cell. https:\/\/doi.org\/10.1016\/j.devcel.2024.09.002 (2024).","DOI":"10.1016\/j.devcel.2024.09.002"},{"key":"55778_CR23","doi-asserted-by":"publisher","unstructured":"Serna, M. et al. CDK5RAP2 activates microtubule nucleator gammaTuRC by facilitating template formation and actin release. Dev. Cell. https:\/\/doi.org\/10.1016\/j.devcel.2024.09.001 (2024).","DOI":"10.1016\/j.devcel.2024.09.001"},{"key":"55778_CR24","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1016\/j.tcb.2014.12.002","volume":"25","author":"TC Lin","year":"2015","unstructured":"Lin, T. C., Neuner, A. & Schiebel, E. Targeting of gamma-tubulin complexes to microtubule organizing centers: conservation and divergence. Trends Cell Biol. 25, 296\u2013307 (2015).","journal-title":"Trends Cell Biol."},{"key":"55778_CR25","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1016\/j.cell.2007.11.043","volume":"132","author":"GJ Brouhard","year":"2008","unstructured":"Brouhard, G. J. et al. XMAP215 is a processive microtubule polymerase. Cell 132, 79\u201388 (2008).","journal-title":"Cell"},{"key":"55778_CR26","doi-asserted-by":"publisher","first-page":"857","DOI":"10.1126\/science.1221698","volume":"337","author":"P Ayaz","year":"2012","unstructured":"Ayaz, P., Ye, X. C., Huddleston, P., Brautigam, C. A. & Rice, L. M. A TOG:\u03b1\u03b2-tubulin complex structure reveals conformation-based mechanisms for a microtubule polymerase. Science 337, 857\u2013860 (2012).","journal-title":"Science"},{"key":"55778_CR27","doi-asserted-by":"publisher","first-page":"28087","DOI":"10.1074\/jbc.M114.584300","volume":"289","author":"M Podolski","year":"2014","unstructured":"Podolski, M., Mahamdeh, M. & Howard, J. Stu2, the budding yeast XMAP215\/Dis1 homolog, promotes assembly of yeast microtubules by increasing growth rate and decreasing catastrophe frequency. J. Biol. Chem. 289, 28087\u201328093 (2014).","journal-title":"J. Biol. Chem."},{"key":"55778_CR28","doi-asserted-by":"publisher","first-page":"e54253","DOI":"10.7554\/eLife.54253","volume":"9","author":"A Thawani","year":"2020","unstructured":"Thawani, A. et al. The transition state and regulation of \u03b3-TuRC-mediated microtubule nucleation revealed by single molecule microscopy. Elife 9, e54253 (2020).","journal-title":"Elife"},{"key":"55778_CR29","doi-asserted-by":"crossref","unstructured":"Gunzelmann, J. et al. The microtubule polymerase Stu2 promotes oligomerization of the gamma-TuSC for cytoplasmic microtubule nucleation. Elife 7, e39932 (2018).","DOI":"10.7554\/eLife.39932"},{"key":"55778_CR30","doi-asserted-by":"publisher","first-page":"1009","DOI":"10.1083\/jcb.200511010","volume":"172","author":"J Al-Bassam","year":"2006","unstructured":"Al-Bassam, J., van Breugel, M., Harrison, S. C. & Hyman, A. Stu2p binds tubulin and undergoes an open-to-closed conformational change. J. Cell Biol. 172, 1009\u20131022 (2006).","journal-title":"J. Cell Biol."},{"key":"55778_CR31","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1038\/s41556-018-0091-6","volume":"20","author":"A Thawani","year":"2018","unstructured":"Thawani, A., Kadzik, R. S. & Petry, S. XMAP215 is a microtubule nucleation factor that functions synergistically with the gamma-tubulin ring complex. Nat. Cell Biol. 20, 575\u2013585 (2018).","journal-title":"Nat. Cell Biol."},{"key":"55778_CR32","doi-asserted-by":"crossref","unstructured":"Ali, A., Vineethakumari, C., Lacasa, C. & L\u00fcders J. Microtubule nucleation and \u03b3TuRC centrosome localization in interphase cells require ch-TOG. Nat. Commun. 14, 289 (2023).","DOI":"10.1038\/s41467-023-35955-w"},{"key":"55778_CR33","doi-asserted-by":"publisher","first-page":"1169","DOI":"10.1083\/jcb.141.5.1169","volume":"141","author":"XP Chen","year":"1998","unstructured":"Chen, X. P., Yin, H. & Huffaker, T. C. The yeast spindle pole body component Spc72p interacts with Stu2p and is required for proper microtubule assembly. J. Cell Biol. 141, 1169\u20131179 (1998).","journal-title":"J. Cell Biol."},{"key":"55778_CR34","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1016\/S0962-8924(02)02268-7","volume":"12","author":"JW Raff","year":"2002","unstructured":"Raff, J. W. Centrosomes and cancer: lessons from a TACC. Trends Cell Biol. 12, 222\u2013225 (2002).","journal-title":"Trends Cell Biol."},{"key":"55778_CR35","doi-asserted-by":"publisher","first-page":"4779","DOI":"10.1093\/emboj\/cdg459","volume":"22","author":"T Usui","year":"2003","unstructured":"Usui, T., Maekawa, H., Pereira, G. & Schiebel, E. The XMAP215 homologue Stu2 at yeast spindle pole bodies regulates microtubule dynamics and anchorage. Embo J. 22, 4779\u20134793 (2003).","journal-title":"Embo J."},{"key":"55778_CR36","doi-asserted-by":"publisher","first-page":"1609","DOI":"10.1091\/mbc.e03-11-0837","volume":"15","author":"M Sato","year":"2004","unstructured":"Sato, M., Vardy, L., Angel Garcia, M., Koonrugsa, N. & Toda, T. Interdependency of fission yeast Alp14\/TOG and coiled coil protein Alp7 in microtubule localization and bipolar spindle formation. Mol. Biol. Cell 15, 1609\u20131622 (2004).","journal-title":"Mol. Biol. Cell"},{"key":"55778_CR37","doi-asserted-by":"publisher","first-page":"546","DOI":"10.1016\/j.cellbi.2007.11.006","volume":"32","author":"N Janski","year":"2008","unstructured":"Janski, N., Herzog, E. & Schmit, A. C. Identification of a novel small Arabidopsis protein interacting with gamma-tubulin complex protein 3. Cell Biol. Int. 32, 546\u2013548 (2008).","journal-title":"Cell Biol. Int"},{"key":"55778_CR38","doi-asserted-by":"publisher","first-page":"593","DOI":"10.1126\/science.1181348","volume":"328","author":"JR Hutchins","year":"2010","unstructured":"Hutchins, J. R. et al. Systematic analysis of human protein complexes identifies chromosome segregation proteins. Science 328, 593\u2013599 (2010).","journal-title":"Science"},{"key":"55778_CR39","doi-asserted-by":"publisher","first-page":"3963","DOI":"10.1091\/mbc.e10-05-0408","volume":"21","author":"N Teixido-Travesa","year":"2010","unstructured":"Teixido-Travesa, N. et al. The gammaTuRC revisited: a comparative analysis of interphase and mitotic human gammaTuRC redefines the set of core components and identifies the novel subunit GCP8. Mol. Biol. Cell 21, 3963\u20133972 (2010).","journal-title":"Mol. Biol. Cell"},{"key":"55778_CR40","doi-asserted-by":"publisher","first-page":"2894","DOI":"10.1091\/mbc.e13-05-0235","volume":"24","author":"H Masuda","year":"2013","unstructured":"Masuda, H., Mori, R., Yukawa, M. & Toda, T. Fission yeast MOZART1\/Mzt1 is an essential \u03b3-tubulin complex component required for complex recruitment to the microtubule organizing center, but not its assembly. Mol. Biol. Cell 24, 2894\u20132906 (2013).","journal-title":"Mol. Biol. Cell"},{"key":"55778_CR41","doi-asserted-by":"publisher","first-page":"1171","DOI":"10.1105\/tpc.111.094904","volume":"24","author":"N Janski","year":"2012","unstructured":"Janski, N. et al. The GCP3-interacting proteins GIP1 and GIP2 are required for \u03b3-tubulin complex protein localization, spindle integrity, and chromosomal stability. Plant Cell 24, 1171\u20131187 (2012).","journal-title":"Plant Cell"},{"key":"55778_CR42","doi-asserted-by":"publisher","first-page":"e2005189","DOI":"10.1371\/journal.pbio.2005189","volume":"16","author":"MD Sallee","year":"2018","unstructured":"Sallee, M. D., Zonka, J. C., Skokan, T. D., Raftrey, B. C. & Feldman, J. L. Tissue-specific degradation of essential centrosome components reveals distinct microtubule populations at microtubule organizing centers. PLoS Biol. 16, e2005189 (2018).","journal-title":"PLoS Biol."},{"key":"55778_CR43","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1083\/jcb.125.1.143","volume":"125","author":"JN McMillan","year":"1994","unstructured":"McMillan, J. N. & Tatchell, K. The JNM1 gene in the yeast Saccharomyces cerevisiae is required for nuclear migration and spindle orientation during the mitotic cell cycle. J. Cell Biol. 125, 143\u2013158 (1994).","journal-title":"J. Cell Biol."},{"key":"55778_CR44","doi-asserted-by":"publisher","first-page":"e108","DOI":"10.1002\/cpbi.108","volume":"72","author":"F Gabler","year":"2020","unstructured":"Gabler, F. et al. Protein sequence analysis using the MPI bioinformatics toolkit. Curr. Protoc. Bioinforma. 72, e108 (2020).","journal-title":"Curr. Protoc. Bioinforma."},{"key":"55778_CR45","doi-asserted-by":"publisher","first-page":"341","DOI":"10.1002\/yea.2967","volume":"30","author":"M Morawska","year":"2013","unstructured":"Morawska, M. & Ulrich, H. D. An expanded tool kit for the auxin\u2010inducible degron system in budding yeast. Yeast 30, 341\u2013351 (2013).","journal-title":"Yeast"},{"key":"55778_CR46","doi-asserted-by":"publisher","first-page":"2809","DOI":"10.1242\/jcs.111.18.2809","volume":"111","author":"S Sou\u00e8s","year":"1998","unstructured":"Sou\u00e8s, S. & Adams, I. R. SPC72: a spindle pole component required for spindle orientation in the yeast Saccharomyces cerevisiae. J. Cell Sci. 111, 2809\u20132818 (1998).","journal-title":"J. Cell Sci."},{"key":"55778_CR47","doi-asserted-by":"publisher","first-page":"1421","DOI":"10.1016\/j.yexcr.2012.03.031","volume":"318","author":"AK Caydasi","year":"2012","unstructured":"Caydasi, A. K. & Pereira, G. SPOC alert-when chromosomes get the wrong direction. Exp. Cell Res. 318, 1421\u20131427 (2012).","journal-title":"Exp. Cell Res."},{"key":"55778_CR48","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1586\/epr.10.109","volume":"8","author":"MJ Chalmers","year":"2011","unstructured":"Chalmers, M. J., Busby, S. A., Pascal, B. D., West, G. M. & Griffin, P. R. Differential hydrogen\/deuterium exchange mass spectrometry analysis of protein-ligand interactions. Expert Rev. Proteom. 8, 43\u201359 (2011).","journal-title":"Expert Rev. Proteom."},{"key":"55778_CR49","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.24340","volume":"6","author":"H Maekawa","year":"2017","unstructured":"Maekawa, H. et al. Polo-like kinase Cdc5 regulates Spc72 recruitment to spindle pole body in the methylotrophic yeast Ogataea polymorpha. eLife 6, e24340 (2017).","journal-title":"eLife"},{"key":"55778_CR50","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.02208","volume":"3","author":"TC Lin","year":"2014","unstructured":"Lin, T. C. et al. Cell-cycle dependent phosphorylation of yeast pericentrin regulates gamma-TuSC-mediated microtubule nucleation. Elife 3, e02208 (2014).","journal-title":"Elife"},{"key":"55778_CR51","doi-asserted-by":"publisher","first-page":"e19700","DOI":"10.1371\/journal.pone.0019700","volume":"6","author":"TC Lin","year":"2011","unstructured":"Lin, T. C. et al. Phosphorylation of the yeast gamma-tubulin Tub4 regulates microtubule function. PLoS One 6, e19700 (2011).","journal-title":"PLoS One"},{"key":"55778_CR52","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-022-28079-0","volume":"13","author":"M Wurtz","year":"2022","unstructured":"Wurtz, M. et al. Modular assembly of the principal microtubule nucleator gamma-TuRC. Nat. Commun. 13, 473 (2022).","journal-title":"Nat. Commun."},{"key":"55778_CR53","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.234799","volume":"132","author":"X Gao","year":"2019","unstructured":"Gao, X. et al. The spindle pole body of Aspergillus nidulans is asymmetrical and contains changing numbers of \u03b3-tubulin complexes. J. Cell Sci. 132, jcs234799 (2019).","journal-title":"J. Cell Sci."},{"key":"55778_CR54","doi-asserted-by":"publisher","first-page":"1505","DOI":"10.1091\/mbc.E19-03-0167","volume":"30","author":"AC Drennan","year":"2019","unstructured":"Drennan, A. C. et al. Structure and function of Spc42 coiled-coils in yeast centrosome assembly and duplication. Mol. Biol. Cell 30, 1505\u20131522 (2019).","journal-title":"Mol. Biol. Cell"},{"key":"55778_CR55","doi-asserted-by":"publisher","first-page":"6475","DOI":"10.1093\/emboj\/19.23.6475","volume":"19","author":"U Gruneberg","year":"2000","unstructured":"Gruneberg, U., Campbell, K., Simpson, C., Grindlay, J. & Schiebel, E. Nud1p links astral microtubule organization and the control of exit from mitosis. EMBO J. 19, 6475\u20136488 (2000).","journal-title":"EMBO J."},{"key":"55778_CR56","doi-asserted-by":"publisher","first-page":"2245","DOI":"10.1091\/mbc.E16-02-0072","volume":"27","author":"AS Lyon","year":"2016","unstructured":"Lyon, A. S. et al. Higher-order oligomerization of Spc110p drives gamma-tubulin ring complex assembly. Mol. Biol. Cell 27, 2245\u20132258 (2016).","journal-title":"Mol. Biol. Cell"},{"key":"55778_CR57","doi-asserted-by":"publisher","DOI":"10.1098\/rsob.200325","volume":"11","author":"M Wurtz","year":"2021","unstructured":"Wurtz, M. et al. Reconstitution of the recombinant human gamma-tubulin ring complex. Open Biol. 11, 200325 (2021).","journal-title":"Open Biol."},{"key":"55778_CR58","doi-asserted-by":"crossref","unstructured":"Zivanov, J. et al. New tools for automated high-resolution cryo-EM structure determination in RELION-3. Elife 7, e42166 (2018).","DOI":"10.7554\/eLife.42166"},{"key":"55778_CR59","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.jsb.2015.11.003","volume":"193","author":"K Zhang","year":"2016","unstructured":"Zhang, K. Gctf: Real-time CTF determination and correction. J. Struct. Biol. 193, 1\u201312 (2016).","journal-title":"J. Struct. Biol."},{"key":"55778_CR60","doi-asserted-by":"publisher","first-page":"963","DOI":"10.1002\/(SICI)1097-0061(199907)15:10B<963::AID-YEA399>3.0.CO;2-W","volume":"15","author":"M Knop","year":"1999","unstructured":"Knop, M. et al. Epitope tagging of yeast genes using a PCR-based strategy: more tags and improved practical routines. Yeast 15, 963\u2013972 (1999).","journal-title":"Yeast"},{"key":"55778_CR61","first-page":"36","volume":"11","author":"MD Abr\u00e0moff","year":"2004","unstructured":"Abr\u00e0moff, M. D., Magalh\u00e3es, P. J. & Ram, S. J. Image processing with ImageJ. Biophotonics Int. 11, 36\u201342 (2004).","journal-title":"Biophotonics Int."},{"key":"55778_CR62","doi-asserted-by":"publisher","first-page":"331","DOI":"10.1038\/nmeth.4193","volume":"14","author":"SQ Zheng","year":"2017","unstructured":"Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331\u2013332 (2017).","journal-title":"Nat. Methods"},{"key":"55778_CR63","doi-asserted-by":"publisher","first-page":"1153","DOI":"10.1038\/s41592-019-0575-8","volume":"16","author":"T Bepler","year":"2019","unstructured":"Bepler, T. et al. Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs. Nat. methods 16, 1153\u20131160 (2019).","journal-title":"Nat. methods"},{"key":"55778_CR64","doi-asserted-by":"publisher","first-page":"290","DOI":"10.1038\/nmeth.4169","volume":"14","author":"A Punjani","year":"2017","unstructured":"Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. methods 14, 290\u2013296 (2017).","journal-title":"Nat. methods"},{"key":"55778_CR65","doi-asserted-by":"publisher","unstructured":"Asarnow, D., Palovcak, E. & Cheng, Y. asarnow\/pyem: UCSF pyem v0.5. Zenodo. https:\/\/doi.org\/10.5281\/zenodo.3576630 (2019).","DOI":"10.5281\/zenodo.3576630"},{"key":"55778_CR66","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1107\/S205225251801463X","volume":"6","author":"J Zivanov","year":"2019","unstructured":"Zivanov, J., Nakane, T. & Scheres, S. H. A Bayesian approach to beam-induced motion correction in cryo-EM single-particle analysis. IUCrJ 6, 5\u201317 (2019).","journal-title":"IUCrJ"},{"key":"55778_CR67","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1107\/S2052252520000081","volume":"7","author":"J Zivanov","year":"2020","unstructured":"Zivanov, J., Nakane, T. & Scheres, S. H. Estimation of high-order aberrations and anisotropic magnification from cryo-EM data sets in RELION-3.1. IUCrJ 7, 253\u2013267 (2020).","journal-title":"IUCrJ"},{"key":"55778_CR68","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.36861","volume":"7","author":"T Nakane","year":"2018","unstructured":"Nakane, T., Kimanius, D., Lindahl, E. & Scheres, S. H. Characterisation of molecular motions in cryo-EM single-particle data by multi-body refinement in RELION. elife 7, e36861 (2018).","journal-title":"elife"},{"key":"55778_CR69","doi-asserted-by":"publisher","first-page":"450","DOI":"10.1038\/s41586-024-07215-4","volume":"628","author":"K Jamali","year":"2024","unstructured":"Jamali, K. et al. Automated model building and protein identification in cryo-EM maps. Nature 628, 450\u2013457 (2024).","journal-title":"Nature"},{"key":"55778_CR70","doi-asserted-by":"publisher","first-page":"D523","DOI":"10.1093\/nar\/gkac1052","volume":"51","author":"C UniProt","year":"2023","unstructured":"UniProt, C. UniProt: the universal protein knowledgebase in 2023. Nucleic Acids Res. 51, D523\u2013D531 (2023).","journal-title":"Nucleic Acids Res"},{"key":"55778_CR71","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1107\/S0907444910007493","volume":"66","author":"P Emsley","year":"2010","unstructured":"Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr D. Biol. Crystallogr 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr D. Biol. Crystallogr"},{"key":"55778_CR72","doi-asserted-by":"publisher","first-page":"861","DOI":"10.1107\/S2059798319011471","volume":"75","author":"D Liebschner","year":"2019","unstructured":"Liebschner, D. et al. Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Acta Crystallogr D. Struct. Biol. 75, 861\u2013877 (2019).","journal-title":"Acta Crystallogr D. Struct. Biol."},{"key":"55778_CR73","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1107\/S2059798318002425","volume":"74","author":"TI Croll","year":"2018","unstructured":"Croll, T. I. ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps. Acta Crystallogr D. Struct. Biol. 74, 519\u2013530 (2018).","journal-title":"Acta Crystallogr D. Struct. Biol."},{"key":"55778_CR74","doi-asserted-by":"publisher","first-page":"1605","DOI":"10.1002\/jcc.20084","volume":"25","author":"EF Pettersen","year":"2004","unstructured":"Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput Chem. 25, 1605\u20131612 (2004).","journal-title":"J. Comput Chem."},{"key":"55778_CR75","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","volume":"596","author":"J Jumper","year":"2021","unstructured":"Jumper, J. et al. Highly accurate protein structure prediction with AlphaFold. Nature 596, 583\u2013589 (2021).","journal-title":"Nature"},{"key":"55778_CR76","doi-asserted-by":"publisher","unstructured":"Evans, R. et al. Protein complex prediction with AlphaFold-Multimer. bioRxiv https:\/\/doi.org\/10.1101\/2021.10.04.463034 (2022).","DOI":"10.1101\/2021.10.04.463034"},{"key":"55778_CR77","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1038\/s41592-022-01488-1","volume":"19","author":"M Mirdita","year":"2022","unstructured":"Mirdita, M. et al. ColabFold: making protein folding accessible to all. Nat. Methods 19, 679\u2013682 (2022).","journal-title":"Nat. Methods"},{"key":"55778_CR78","doi-asserted-by":"publisher","first-page":"301","DOI":"10.1042\/EBC20220111","volume":"67","author":"V Vinciauskaite","year":"2023","unstructured":"Vinciauskaite, V. & Masson, G. R. Fundamentals of HDX-MS. Essays Biochem 67, 301\u2013314 (2023).","journal-title":"Essays Biochem"},{"key":"55778_CR79","doi-asserted-by":"publisher","first-page":"2669","DOI":"10.1083\/jcb.201612195","volume":"216","author":"SC Howes","year":"2017","unstructured":"Howes, S. C. et al. Structural differences between yeast and mammalian microtubules revealed by cryo-EM. J. Cell Biol. 216, 2669\u20132677 (2017).","journal-title":"J. Cell Biol."},{"key":"55778_CR80","doi-asserted-by":"publisher","first-page":"e38922","DOI":"10.7554\/eLife.38922","volume":"7","author":"S Nithianantham","year":"2018","unstructured":"Nithianantham, S. et al. Structural basis of tubulin recruitment and assembly by microtubule polymerases with tumor overexpressed gene (TOG) domain arrays. Elife 7, e38922 (2018).","journal-title":"Elife"}],"container-title":["Nature Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-55778-7.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-55778-7","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-55778-7.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,1,5]],"date-time":"2025-01-05T09:02:40Z","timestamp":1736067760000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-55778-7"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,1,5]]},"references-count":80,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["55778"],"URL":"https:\/\/doi.org\/10.1038\/s41467-024-55778-7","relation":{},"ISSN":["2041-1723"],"issn-type":[{"value":"2041-1723","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,1,5]]},"assertion":[{"value":"10 April 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"24 December 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 January 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"402"}}