期刊
CELL REPORTS
卷 31, 期 13, 页码 -出版社
CELL PRESS
DOI: 10.1016/j.celrep.2020.107791
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资金
- NIH [R35 GM130234]
- HFSP fellowship [LT000025/18-L1]
- Rockefeller University's Pels Center for Biochemistry and Structural Biology
- Ministry of Science and Technology [MOST-106-2311-B-001-038-MY3]
- Academia Sinica [AS-CDA-106-L02]
Microtubule organization depends on the gamma-tubulin ring complex (gamma-TuRC), a similar to 2.3-MDa nucleation factor comprising an asymmetric assembly of gamma-tubulin and GCP2-GCP6. However, it is currently unclear how the gamma-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 gamma-TURC. MZT1 forms two subcomplexes with the N-terminal alpha-helical domains of GCP3 or GCP6 (GCP-NHDs) within the gamma-TuRC lumenal bridge. We determine the X-ray structure of recombinant MZT1/GCP6-NHD and find it is similar to that within the native gamma-TuRC. We identify two additional MZT/GCP-NHD-like subcomplexes, one of which is located on the outer face of the gamma-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 gamma-TuRC.
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