Membrane association and remodeling by intraflagellar transport protein IFT172.

Details

Ressource 1Download: s41467-018-07037-9.pdf (6372.38 [Ko])
State: Public
Version: Final published version
Serval ID
serval:BIB_9E42AE74B0C0
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Membrane association and remodeling by intraflagellar transport protein IFT172.
Journal
Nature communications
Author(s)
Wang Q., Taschner M., Ganzinger K.A., Kelley C., Villasenor A., Heymann M., Schwille P., Lorentzen E., Mizuno N.
ISSN
2041-1723 (Electronic)
ISSN-L
2041-1723
Publication state
Published
Issued date
08/11/2018
Peer-reviewed
Oui
Volume
9
Number
1
Pages
4684
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
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.
Keywords
Bacterial Proteins/chemistry, Bacterial Proteins/metabolism, Bacterial Proteins/ultrastructure, Cell Membrane/metabolism, Cell Membrane/ultrastructure, Chlamydomonas, Flagella/metabolism, Lipids/chemistry, Liposomes, Membrane Proteins/chemistry, Membrane Proteins/metabolism, Protein Binding, Protein Conformation, Recombinant Proteins/metabolism
Pubmed
Web of science
Open Access
Yes
Create date
16/11/2018 11:02
Last modification date
20/08/2019 15:04
Usage data