6u42
From Proteopedia
Natively decorated ciliary doublet microtubule
Structural highlights
Function[TBA1_CHLRE] 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. [TBB_CHLRE] 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. [ODA1_CHLRE] Component of the outer dynein arm complex required for assembly of the outer dynein arm-docking complex (ODA-DC) and the outer dynein arm onto the doublet microtubule.[1] [FLTOP_CHLRE] May act as a regulator of cilium basal body docking and positioning in mono- and multiciliated cells.[UniProtKB:Q6P8X9] [CFA20_CHLRE] Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility (PubMed:24259666, PubMed:24574454). Involved in the control of flagellar beating in an asymmetric and planar waveform (PubMed:24259666, PubMed:24574454). Stabilizes outer doublet microtubules (DMTs) of the axoneme and may work as a scaffold for intratubular proteins, such as tektin and PACRG, to produce the beak structures in DMT1, 5 and 6 (PubMed:24259666, PubMed:24574454). Not essential for flagellar assembly (PubMed:24574454).[2] [3] [CFA53_CHLRE] May play a role in filopodium movement.[UniProtKB:Q96M91] Publication Abstract from PubMedThe axoneme of motile cilia is the largest macromolecular machine of eukaryotic cells. In humans, impaired axoneme function causes a range of ciliopathies. Axoneme assembly, structure, and motility require a radially arranged set of doublet microtubules, each decorated in repeating patterns with non-tubulin components. We use single-particle cryo-electron microscopy to visualize and build an atomic model of the repeating structure of a native axonemal doublet microtubule, which reveals the identities, positions, repeat lengths, and interactions of 38 associated proteins, including 33 microtubule inner proteins (MIPs). The structure demonstrates how these proteins establish the unique architecture of doublet microtubules, maintain coherent periodicities along the axoneme, and stabilize the microtubules against the repeated mechanical stress induced by ciliary motility. Our work elucidates the architectural principles that underpin the assembly of this large, repetitive eukaryotic structure and provides a molecular basis for understanding the etiology of human ciliopathies. Structure of the Decorated Ciliary Doublet Microtubule.,Ma M, Stoyanova M, Rademacher G, Dutcher SK, Brown A, Zhang R Cell. 2019 Oct 31;179(4):909-922.e12. doi: 10.1016/j.cell.2019.09.030. Epub 2019 , Oct 24. PMID:31668805[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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