MZT Proteins Form Multi-Faceted Structural Modules in the γ-Tubulin Ring Complex
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2020-06-30
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Journal Article
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Abstract
Microtubule organization depends on the g-tubulin ring complex (g-TuRC), a 2.3-MDa nucleation factor comprising an asymmetric assembly of g-tubulin and GCP2-GCP6. However, it is currently unclear how the g-TuRC-associated microproteins MZT1 and MZT2 contribute to the structure and regulation of the holocomplex. Here, we report cryo-EM structures of MZT1 and MZT2 in the context of the native human g-TuRC. MZT1 forms two subcomplexes with the N-terminal a-helical domains of GCP3 or GCP6 (GCP-NHDs) within the g-TuRC ‘‘lumenal bridge.’’ We determine the X-ray structure of recombinant MZT1/GCP6-NHD and find it is similar to that within the native g-TuRC. We identify two additional MZT/GCP-NHD-like subcomplexes, one of which is located on the outer face of the g-TuRC and comprises MZT2 and GCP2-NHD in complex with a centrosomin motif 1 (CM1)-containing peptide. Our data reveal how MZT1 and MZT2 establish multi-faceted, structurally mimetic ‘‘modules’’ that can expand structural and regulatory interfaces in the g-TuRC.
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31 (13)
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107791
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Cell Press
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09763 - Wieczorek, Michal / Wieczorek, Michal