STORM imaging reveals the spatial arrangement of transition zone components and IFT particles at the ciliary base in Tetrahymena

Autor:	Zhu Zhou, Jarema Malicki, Natalia A. Bulgakova, Dorota Wloga, Khodor S. Hazime, Ewa Joachimiak
Jazyk:	angličtina
Rok vydání:	2021
Předmět:	Protozoan Proteins/metabolism Mutation/genetics Science Protozoan Proteins Tetrahymena/metabolism Article Imaging Ciliopathies/genetics Cilia/metabolism Intraflagellar transport DOCK Developmental biology Genetics Sequencing Humans Cilia Ciliary membrane Bardet-Biedl Syndrome Biological models Flagella/metabolism Ciliate Microscopy Multidisciplinary biology Ciliogenesis Chemistry Cilium Compartment (ship) Biological techniques Tetrahymena Biological Transport Bardet-Biedl Syndrome/metabolism biology.organism_classification Ciliopathies Computational biology and bioinformatics Flagella Mutation Biophysics Medicine sense organs Ciliary base Software Microscopy/methods
Zdroj:	Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021) Hazime, K 2021, ' STORM imaging reveals the spatial arrangement of transition zone components and IFT particles at the ciliary base in Tetrahymena ', Scientific Reports, vol. 11, no. 1, 7899 . https://doi.org/10.1038/s41598-021-86909-5 Scientific Reports
ISSN:	2045-2322
DOI:	10.1038/s41598-021-86909-5
Popis:	The base of the cilium comprising the transition zone (TZ) and transition fibers (TF) acts as a selecting gate to regulate the intraflagellar transport (IFT)-dependent trafficking of proteins to and from cilia. Before entering the ciliary compartment, IFT complexes and transported cargoes accumulate at or near the base of the cilium. The spatial organization of IFT proteins at the cilia base is key for understanding cilia formation and function. Using stochastic optical reconstruction microscopy (STORM) and computational averaging, we show that seven TZ, nine IFT, three Bardet–Biedl syndrome (BBS), and one centrosomal protein, form 9-clustered rings at the cilium base of a ciliate Tetrahymena thermophila. In the axial dimension, analyzed TZ proteins localize to a narrow region of about 30 nm while IFT proteins dock approximately 80 nm proximal to TZ. Moreover, the IFT-A subcomplex is positioned peripheral to the IFT-B subcomplex and the investigated BBS proteins localize near the ciliary membrane. The positioning of the HA-tagged N- and C-termini of the selected proteins enabled the prediction of the spatial orientation of protein particles and likely cargo interaction sites. Based on the obtained data, we built a comprehensive 3D-model showing the arrangement of the investigated ciliary proteins.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5acfd215b41b18c3ff92811e9643cce https://doaj.org/article/ad03647e47844e35a88866b74e826023 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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