Membrane association and remodeling by intraflagellar transport protein IFT172

Qianmin Wang, Michael Taschner, Kristina A. Ganzinger, Charlotte Kelley, Alethia Villasenor, Michael Heymann, Petra Schwille, Esben Lorentzen () and Naoko Mizuno ()
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Qianmin Wang: Max Planck Institute of Biochemistry, Department of Structural Cell Biology
Michael Taschner: Max Planck Institute of Biochemistry, Department of Structural Cell Biology
Kristina A. Ganzinger: Max Planck Institute of Biochemistry, Department of Cellular and Molecular Biophysics
Charlotte Kelley: Max Planck Institute of Biochemistry, Department of Structural Cell Biology
Alethia Villasenor: Max Planck Institute of Biochemistry, Department of Structural Cell Biology
Michael Heymann: Max Planck Institute of Biochemistry, Department of Cellular and Molecular Biophysics
Petra Schwille: Max Planck Institute of Biochemistry, Department of Cellular and Molecular Biophysics
Esben Lorentzen: Aarhus University
Naoko Mizuno: Max Planck Institute of Biochemistry, Department of Structural Cell Biology

Nature Communications, 2018, vol. 9, issue 1, 1-13

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-07037-9

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