Membrane association and remodeling by intraflagellar transport protein IFT172

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

Membrane association and remodeling by intraflagellar transport protein IFT172. / Wang, Qianmin; Taschner, Michael; Ganzinger, Kristina A; Kelley, Charlotte; Villasenor, Alethia; Heymann, Michael; Schwille, Petra; Lorentzen, Esben; Mizuno, Naoko.

I: Nature Communications, Bind 9, Nr. 1, 4684, 08.11.2018.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Wang, Q, Taschner, M, Ganzinger, KA, Kelley, C, Villasenor, A, Heymann, M, Schwille, P, Lorentzen, E & Mizuno, N 2018, 'Membrane association and remodeling by intraflagellar transport protein IFT172', Nature Communications, bind 9, nr. 1, 4684. https://doi.org/10.1038/s41467-018-07037-9

APA

Wang, Q., Taschner, M., Ganzinger, K. A., Kelley, C., Villasenor, A., Heymann, M., Schwille, P., Lorentzen, E., & Mizuno, N. (2018). Membrane association and remodeling by intraflagellar transport protein IFT172. Nature Communications, 9(1), [4684]. https://doi.org/10.1038/s41467-018-07037-9

CBE

Wang Q, Taschner M, Ganzinger KA, Kelley C, Villasenor A, Heymann M, Schwille P, Lorentzen E, Mizuno N. 2018. Membrane association and remodeling by intraflagellar transport protein IFT172. Nature Communications. 9(1):Article 4684. https://doi.org/10.1038/s41467-018-07037-9

MLA

Vancouver

Wang Q, Taschner M, Ganzinger KA, Kelley C, Villasenor A, Heymann M o.a. Membrane association and remodeling by intraflagellar transport protein IFT172. Nature Communications. 2018 nov 8;9(1). 4684. https://doi.org/10.1038/s41467-018-07037-9

Author

Wang, Qianmin ; Taschner, Michael ; Ganzinger, Kristina A ; Kelley, Charlotte ; Villasenor, Alethia ; Heymann, Michael ; Schwille, Petra ; Lorentzen, Esben ; Mizuno, Naoko. / Membrane association and remodeling by intraflagellar transport protein IFT172. I: Nature Communications. 2018 ; Bind 9, Nr. 1.

Bibtex

@article{2b6636a9406443d8a21d7e6add704311,
title = "Membrane association and remodeling by intraflagellar transport protein IFT172",
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.",
author = "Qianmin Wang and Michael Taschner and Ganzinger, {Kristina A} and Charlotte Kelley and Alethia Villasenor and Michael Heymann and Petra Schwille and Esben Lorentzen and Naoko Mizuno",
year = "2018",
month = nov,
day = "8",
doi = "10.1038/s41467-018-07037-9",
language = "English",
volume = "9",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",

}

RIS

TY - JOUR

T1 - Membrane association and remodeling by intraflagellar transport protein IFT172

AU - Wang, Qianmin

AU - Taschner, Michael

AU - Ganzinger, Kristina A

AU - Kelley, Charlotte

AU - Villasenor, Alethia

AU - Heymann, Michael

AU - Schwille, Petra

AU - Lorentzen, Esben

AU - Mizuno, Naoko

PY - 2018/11/8

Y1 - 2018/11/8

N2 - 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.

AB - 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.

U2 - 10.1038/s41467-018-07037-9

DO - 10.1038/s41467-018-07037-9

M3 - Journal article

C2 - 30409972

VL - 9

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 4684

ER -