Crystal structure of γ-tubulin complex protein GCP4 provides insight into microtubule nucleation
| Autor: | Martine Knibiehler, Valérie Guillet, Cécile Chemin, Marie-Hélène Remy, Justin M. Kollman, Andreas Merdes, Lynn Gregory-Pauron, David A. Agard, Lionel Mourey, Cécile Bon, Brigitte Raynaud-Messina |
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| Přispěvatelé: | Institut de pharmacologie et de biologie structurale (IPBS), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées |
| Rok vydání: | 2011 |
| Předmět: |
Microtubule-associated protein
[SDV]Life Sciences [q-bio] Protein domain macromolecular substances Biology Crystallography X-Ray Microtubules Article 03 medical and health sciences 0302 clinical medicine Protein structure Tubulin Structural Biology Microtubule Humans Protein Interaction Domains and Motifs Molecular Biology 030304 developmental biology Microtubule nucleation 0303 health sciences Tubulin complex Binding Sites Protein tertiary structure Protein Structure Tertiary Crystallography biology.protein Microtubule-Associated Proteins 030217 neurology & neurosurgery |
| Zdroj: | Nature Structural and Molecular Biology Nature Structural and Molecular Biology, Nature Publishing Group, 2011, 18, pp.915-919. ⟨10.1038/nsmb.2083⟩ |
| ISSN: | 1545-9985 1545-9993 |
| DOI: | 10.1038/nsmb.2083 |
| Popis: | International audience; Microtubule nucleation in all eukaryotes involves g-tubulin small complexes (gTuSCs) that comprise two molecules of g-tubulin bound to g-tubulin complex proteins (GCPs) GCP2 and GCP3. In many eukaryotes, multiple gTuSCs associate with GCP4, GCP5 and GCP6 into large g-tubulin ring complexes (gTuRCs). Recent cryo-EM studies indicate that a scaffold similar to gTuRCs is formed by lateral association of gTuSCs, with the C-terminal regions of GCP2 and GCP3 binding g-tubulin molecules. However, the exact role of GCPs in microtubule nucleation remains unknown. Here we report the crystal structure of human GCP4 and show that its C-terminal domain binds directly to g-tubulin. The human GCP4 structure is the prototype for all GCPs, as it can be precisely positioned within the gTuSC envelope, revealing the nature of protein-protein interactions and conformational changes regulating nucleation activity. |
| Databáze: | OpenAIRE |
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