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  Membrane association and remodeling by intraflagellar transport protein IFT172

Wang, Q., Taschner, M., Ganzinger, K. A., Kelley, C., Villasenor, A., Heymann, M., et al. (2018). Membrane association and remodeling by intraflagellar transport protein IFT172. Nature Communications, 9: 4684. doi:10.1038/s41467-018-07037-9.

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 Creators:
Wang, Qianmin1, Author           
Taschner, Michael2, Author           
Ganzinger, Kristina A.3, Author           
Kelley, Charlotte2, Author           
Villasenor, Alethia2, Author           
Heymann, Michael3, Author           
Schwille, Petra3, Author           
Lorentzen, Esben4, Author
Mizuno, Naoko1, Author           
Affiliations:
1Mizuno, Naoko / Cellular and Membrane Trafficking, Max Planck Institute of Biochemistry, Max Planck Society, ou_1688137              
2Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
3Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              
4external, ou_persistent22              

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Free keywords: CHLAMYDOMONAS-REINHARDTII; EXTRACELLULAR VESICLES; ELECTRON-MICROSCOPY; EUKARYOTIC CILIUM; SENSORY NEURONS; FLAGELLAR TIP; CILIARY; COMPLEX; CELLS; MICROTUBULESScience & Technology - Other Topics;
 Abstract: The cilium is an organelle used for motility and cellular signaling. Intraflagellar transport (IFT) is a process to move ciliary building blocks and signaling components into the cilium. How IFT controls the movement of ciliary components is currently poorly understood. IFT172 is the largest IFT subunit essential for ciliogenesis. Due to its large size, the characterization of IFT172 has been challenging. Using giant unilamellar vesicles (GUVs), we show that IFT172 is a membrane-interacting protein with the ability to remodel large membranes into small vesicles. Purified IFT172 has an architecture of two globular domains with a long rod-like protrusion, resembling the domain organization of coatomer proteins such as COPI-II or clathrin. IFT172 adopts two different conformations that can be manipulated by lipids or detergents: 1) an extended elongated conformation and 2) a globular closed architecture. Interestingly, the association of IFT172 with membranes is mutually exclusive with IFT57, implicating multiple functions for IFT172 within IFT.

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Language(s): eng - English
 Dates: 2018
 Publication Status: Published online
 Pages: 13
 Publishing info: -
 Table of Contents: We also thank MPI-B biochemistry core and imaging facility for their help and instrumental service.
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Project name : (724209 for N.M.)
Grant ID : 724209
Funding program : -
Funding organization : European Research Council (EC)
Project name : (310343 for E.L.)
Grant ID : 310343
Funding program : -
Funding organization : European Research Council/International
Project name : Research of N.M. is supported by Boehringer Ingelheim plus3 program as well as DFG 1745 1/2, GRK1721. E.L. is supported by Novo Nordisk Foundation (grant no. NNF15OC0014164).
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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 9 Sequence Number: 4684 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723