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Tubulin lattice in cilia is in a stressed form regulated by microtubule inner proteins

Ichikawa, Muneyoshi ; Khalifa, Ahmad Abdelzaher Zaki ; Kubo, Shintaroh ; Dai, Daniel ; Basu, Kaustuv ; Maghrebi, Mohammad Amin Faghfor ; Vargas, Javier ; Bui, Khanh Huy

Proceedings of the National Academy of Sciences - PNAS, 2019-10, Vol.116 (40), p.19930-19938 [Periódico revisado por pares]

United States: National Academy of Sciences

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Título:
Tubulin lattice in cilia is in a stressed form regulated by microtubule inner proteins
Autor: Ichikawa, Muneyoshi ; Khalifa, Ahmad Abdelzaher Zaki ; Kubo, Shintaroh ; Dai, Daniel ; Basu, Kaustuv ; Maghrebi, Mohammad Amin Faghfor ; Vargas, Javier ; Bui, Khanh Huy
Assuntos: Axoneme - chemistry ; Biological Sciences ; Cilia ; Cilia - chemistry ; Cryoelectron Microscopy ; Cytoskeleton - chemistry ; Dimers ; Mass Spectrometry ; Mass spectroscopy ; Microscopy ; Microtubule Proteins - chemistry ; Microtubules ; Microtubules - chemistry ; Molecular Dynamics Simulation ; Molecular structure ; Paclitaxel - chemistry ; Protein Binding ; Protein Conformation ; Protein Multimerization ; Protein Structure, Secondary ; Proteins ; Protozoan Proteins - chemistry ; Sheaths ; Stress, Mechanical ; Tetrahymena - chemistry ; Tubulin ; Tubulin - chemistry ; Waveforms
É parte de: Proceedings of the National Academy of Sciences - PNAS, 2019-10, Vol.116 (40), p.19930-19938
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
1M.I. and A.A.Z.K. contributed equally to this work.
2Present address: Department of Systems Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.
Author contributions: M.I. and K.H.B. designed research; M.I., A.A.Z.K., S.K., and K.B. performed research; J.V. contributed new reagents/analytic tools; M.I., A.A.Z.K., S.K., D.D., M.A.F.M., and K.H.B. analyzed data; and M.I., A.A.Z.K., D.D., and K.H.B. wrote the paper.
Edited by Takashi Ishikawa, Paul Scherrer Institut (PSI), Villigen PSI, Switzerland, and accepted by Editorial Board Member Yale E. Goldman August 22, 2019 (received for review July 2, 2019)
Descrição: Cilia, the hair-like protrusions that beat at high frequencies to propel a cell or move fluid around are composed of radially bundled doublet microtubules. In this study, we present a near-atomic resolution map of the Tetrahymena doublet microtubule by cryoelectron microscopy. The map demonstrates that the network of microtubule inner proteins weaves into the tubulin lattice and forms an inner sheath. From mass spectrometry data and de novo modeling, we identified Rib43a proteins as the filamentous microtubule inner proteins in the protofilament ribbon region. The Rib43a–tubulin interaction leads to an elongated tubulin dimer distance every 2 dimers. In addition, the tubulin lattice structure with missing microtubule inner proteins (MIPs) by sarkosyl treatment shows significant longitudinal compaction and lateral angle change between protofilaments. These results are evidence that the MIPs directly affect and stabilize the tubulin lattice. It suggests that the doublet microtubule is an intrinsically stressed filament and that this stress could be manipulated in the regulation of ciliary waveforms.
Editor: United States: National Academy of Sciences
Idioma: Inglês

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Tubulin lattice in cilia is in a stressed form regulated by microtubule inner proteins

Ichikawa, Muneyoshi ; Khalifa, Ahmad Abdelzaher Zaki ; Kubo, Shintaroh ; Dai, Daniel ; Basu, Kaustuv ; Maghrebi, Mohammad Amin Faghfor ; Vargas, Javier ; Bui, Khanh Huy

United States: National Academy of Sciences

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