Fiche du document
8 novembre 2018
- doi: 10.1038/s41467-018-07037-9
- issn: 2041-1723
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/doi/10.1038/s41467-018-07037-9
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pmid/30409972
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/eissn/2041-1723
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_9E42AE74B0C05
info:eu-repo/semantics/openAccess , Copying allowed only for non-profit organizations , https://serval.unil.ch/disclaimer
Sujets proches
Transportation industry Transport Transportation companies Transportation--Economic aspects Transportation, Primitive Public transportation Group dynamics Association Groups, Social Western architecture (Western countries) Building design Construction Buildings--Design and construction Architecture, Western (Western countries) circulationCiter ce document
Q. Wang et al., « Membrane association and remodeling by intraflagellar transport protein IFT172. », Serveur académique Lausannois, ID : 10.1038/s41467-018-07037-9
Métriques
Partage / Export
Résumé
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.