FAP106 Is an Interaction Hub for Assembling Microtubule Inner Proteins at the Cilium Inner Junction. Shimogawa, M. M., Wijono, A. S., Wang, H., Zhang, J., Sha, J., Szombathy, N., Vadakkan, S., Pelayo, P., Jonnalagadda, K., Wohlschlegel, J., Zhou, Z. H., & Hill, K. L. Nature Communications, 14(1):5225, Nature Publishing Group, August, 2023. doi abstract bibtex Motility of pathogenic protozoa depends on flagella (synonymous with cilia) with axonemes containing nine doublet microtubules (DMTs) and two singlet microtubules. Microtubule inner proteins (MIPs) within DMTs influence axoneme stability and motility and provide lineage-specific adaptations, but individual MIP functions and assembly mechanisms are mostly unknown. Here, we show in the sleeping sickness parasite Trypanosoma brucei, that FAP106, a conserved MIP at the DMT inner junction, is required for trypanosome motility and functions as a critical interaction hub, directing assembly of several conserved and lineage-specific MIPs. We use comparative cryogenic electron tomography (cryoET) and quantitative proteomics to identify MIP candidates. Using RNAi knockdown together with fitting of AlphaFold models into cryoET maps, we demonstrate that one of these candidates, MC8, is a trypanosome-specific MIP required for parasite motility. Our work advances understanding of MIP assembly mechanisms and identifies lineage-specific motility proteins that are attractive targets to consider for therapeutic intervention.
@article{shimogawaFAP106InteractionHub2023,
title = {{{FAP106}} Is an Interaction Hub for Assembling Microtubule Inner Proteins at the Cilium Inner Junction},
author = {Shimogawa, Michelle M. and Wijono, Angeline S. and Wang, Hui and Zhang, Jiayan and Sha, Jihui and Szombathy, Natasha and Vadakkan, Sabeeca and Pelayo, Paula and Jonnalagadda, Keya and Wohlschlegel, James and Zhou, Z. Hong and Hill, Kent L.},
year = {2023},
month = aug,
journal = {Nature Communications},
volume = {14},
number = {1},
pages = {5225},
publisher = {Nature Publishing Group},
issn = {2041-1723},
doi = {10.1038/s41467-023-40230-z},
urldate = {2024-06-13},
abstract = {Motility of pathogenic protozoa depends on flagella (synonymous with cilia) with axonemes containing nine doublet microtubules (DMTs) and two singlet microtubules. Microtubule inner proteins (MIPs) within DMTs influence axoneme stability and motility and provide lineage-specific adaptations, but individual MIP functions and assembly mechanisms are mostly unknown. Here, we show in the sleeping sickness parasite Trypanosoma brucei, that FAP106, a conserved MIP at the DMT inner junction, is required for trypanosome motility and functions as a critical interaction hub, directing assembly of several conserved and lineage-specific MIPs. We use comparative cryogenic electron tomography (cryoET) and quantitative proteomics to identify MIP candidates. Using RNAi knockdown together with fitting of AlphaFold models into cryoET maps, we demonstrate that one of these candidates, MC8, is a trypanosome-specific MIP required for parasite motility. Our work advances understanding of MIP assembly mechanisms and identifies lineage-specific motility proteins that are attractive targets to consider for therapeutic intervention.},
copyright = {2023 The Author(s)},
langid = {english},
keywords = {Cellular motility,Cilia,cryoET,Microtubules,Parasite biology},
file = {C:\Users\shervinnia\Zotero\storage\28SPTW4N\Shimogawa et al. - 2023 - FAP106 is an interaction hub for assembling microt.pdf}
}
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