生物
微管
蛋白质组
鞭毛
细胞生物学
蛋白质组学
精子
微管相关蛋白
对接(动物)
动力蛋白
计算生物学
生物信息学
生物化学
遗传学
基因
医学
护理部
作者
Zhe Chen,Momoko Shiozaki,Kelsey M. Haas,Will M. Skinner,Shumei Zhao,Caiying Guo,Benjamin J. Polacco,Zhiheng Yu,Nevan J. Krogan,Polina V. Lishko,Robyn M. Kaake,Ronald D. Vale,David A. Agard
出处
期刊:Cell
[Elsevier]
日期:2023-11-01
卷期号:186 (23): 5041-5053.e19
被引量:7
标识
DOI:10.1016/j.cell.2023.09.017
摘要
Summary
To understand the molecular mechanisms of cellular pathways, contemporary workflows typically require multiple techniques to identify proteins, track their localization, and determine their structures in vitro. Here, we combined cellular cryoelectron tomography (cryo-ET) and AlphaFold2 modeling to address these questions and understand how mammalian sperm are built in situ. Our cellular cryo-ET and subtomogram averaging provided 6.0-Å reconstructions of axonemal microtubule structures. The well-resolved tertiary structures allowed us to unbiasedly match sperm-specific densities with 21,615 AlphaFold2-predicted protein models of the mouse proteome. We identified Tektin 5, CCDC105, and SPACA9 as novel microtubule-associated proteins. These proteins form an extensive interaction network crosslinking the lumen of axonemal doublet microtubules, suggesting their roles in modulating the mechanical properties of the filaments. Indeed, Tekt5 −/− sperm possess more deformed flagella with 180° bends. Together, our studies presented a cellular visual proteomics workflow and shed light on the in vivo functions of Tektin 5.
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