Abstract
Multi-subunit tethering complexes (MTCs) are a family of evolutionarily conserved large protein complexes that function to tether intracellular vesicles from the donor compartments to the membrane of receptor compartments. The exocyst complex is an octameric MTC that tethers the post-Golgi secretory vesicles to the plasma membrane. To learn the function and regulation of the exocyst complex, it is crucial to understand the structure of the complex. We have solved the cryo-EM structure of the exocyst complex at 4.4 Angstrom (Å) resolution and detected the spatial relationship between the eight subunits using chemical cross-linking mass spectrometry. Here, we describe the method of modeling and validating the cryo-EM structure of the exocyst complex. This method could provide a guide for modeling of other protein complexes of which the structures are solved at medium to near-atomic resolution.
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Acknowledgment
We thank Yirong Liu for helpful suggestions. This work is supported by National Institutes of Health grant R35GM141832 to W.G., National Science Foundation of China (Grant 91954112 and 31900501), and Young Elite Scientists Sponsorship Program by Tianjin (TJSQNTJ-2020-19) to K.M.
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Mei, K., Guo, W. (2023). Modeling the Cryo-EM Structure of the Exocyst Complex. In: Wang, Y., Lupashin, V.V., Graham, T.R. (eds) Golgi. Methods in Molecular Biology, vol 2557. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2639-9_16
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DOI: https://doi.org/10.1007/978-1-0716-2639-9_16
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