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Cryo-EM structure of ciliary microtubule doubletCryo-EM structure of ciliary microtubule doublet
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Structural highlights
FunctionTBA_TETTH Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Publication Abstract from PubMedCilia are ubiquitous, hair-like appendages found in eukaryotic cells that carry out functions of cell motility and sensory reception. Cilia contain an intriguing cytoskeletal structure, termed the axoneme that consists of nine doublet microtubules radially interlinked and longitudinally organized in multiple specific repeat units. Little is known, however, about how the axoneme allows cilia to be both actively bendable and sturdy or how it is assembled. To answer these questions, we used cryo-electron microscopy to structurally analyse several of the repeating units of the doublet at sub-nanometre resolution. This structural detail enables us to unambiguously assign alpha- and beta-tubulins in the doublet microtubule lattice. Our study demonstrates the existence of an inner sheath composed of different kinds of microtubule inner proteins inside the doublet that likely stabilizes the structure and facilitates the specific building of the B-tubule. Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins.,Ichikawa M, Liu D, Kastritis PL, Basu K, Hsu TC, Yang S, Bui KH Nat Commun. 2017 May 2;8:15035. doi: 10.1038/ncomms15035. PMID:28462916[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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