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Journal Article

Membrane association and remodeling by intraflagellar transport protein IFT172

MPS-Authors
/persons/resource/persons134789

Wang,  Qianmin
Mizuno, Naoko / Cellular and Membrane Trafficking, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78783

Taschner,  Michael
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons192369

Ganzinger,  Kristina A.
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons229879

Kelley,  Charlotte
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons229887

Villasenor,  Alethia
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons197087

Heymann,  Michael
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons15815

Schwille,  Petra
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78408

Mizuno,  Naoko
Mizuno, Naoko / Cellular and Membrane Trafficking, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource

https://www.nature.com/articles/s41467-018-07037-9#Sec23
(Supplementary material)

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Fulltext (public)

s41467-018-07037-9.pdf
(Publisher version), 7MB

Supplementary Material (public)

41467_2018_7037_MOESM1_ESM.pdf
(Supplementary material), 5MB

Citation

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.


Cite as: https://hdl.handle.net/21.11116/0000-0002-EDFC-8
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.