Membrane association and remodeling by intraflagellar transport protein IFT172

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  • Qianmin Wang, Department of Structural Cell Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
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  • Michael Taschner, Department of Structural Cell Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
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  • Kristina A Ganzinger, AMOLF, Living Matter Department, Science Park 104, 1098 XG, Amsterdam, The Netherlands.
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  • Charlotte Kelley, Department of Structural Cell Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
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  • Alethia Villasenor, Department of Structural Cell Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
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  • Michael Heymann, Max Planck Institute of Biochemistry, Department of Cellular and Molecular Biophysics, Am Klopferspitz 18, D-82152, Martinsried, Germany.
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  • Petra Schwille, Max Planck Institute of Biochemistry, Department of Cellular and Molecular Biophysics, Am Klopferspitz 18, D-82152, Martinsried, Germany.
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  • Esben Lorentzen
  • Naoko Mizuno, Max Planck Institute of Biochemistry, Department of Structural Cell Biology, Am Klopferspitz 18, D-82152, Martinsried, Germany. mizuno@biochem.mpg.de.

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.

Original languageEnglish
Article number4684
JournalNature Communications
Volume9
Issue1
ISSN2041-1723
DOIs
Publication statusPublished - 8 Nov 2018

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