The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K

The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K

TMEM16K is a member of the TMEM16 family of integral membrane proteins that are either lipid scramblases or chloride channels. Here the authors combine cell biology, electrophysiology measurements, X-ray crystallography, cryo-EM and MD simulations to structurally characterize TMEM16K and show that i...

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Autores principales: Simon R. Bushell, Ashley C. W. Pike, Maria E. Falzone, Nils J. G. Rorsman, Chau M. Ta, Robin A. Corey, Thomas D. Newport, John C. Christianson, Lara F. Scofano, Chitra A. Shintre, Annamaria Tessitore, Amy Chu, Qinrui Wang, Leela Shrestha, Shubhashish M. M. Mukhopadhyay, James D. Love, Nicola A. Burgess-Brown, Rebecca Sitsapesan, Phillip J. Stansfeld, Juha T. Huiskonen, Paolo Tammaro, Alessio Accardi, Elisabeth P. Carpenter
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Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/602dd2cc133c49529d8807b7b0d875ca
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spelling oai:doaj.org-article:602dd2cc133c49529d8807b7b0d875ca2021-12-02T14:39:38ZThe structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K10.1038/s41467-019-11753-12041-1723https://doaj.org/article/602dd2cc133c49529d8807b7b0d875ca2019-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11753-1https://doaj.org/toc/2041-1723TMEM16K is a member of the TMEM16 family of integral membrane proteins that are either lipid scramblases or chloride channels. Here the authors combine cell biology, electrophysiology measurements, X-ray crystallography, cryo-EM and MD simulations to structurally characterize TMEM16K and show that it is an ER-resident lipid scramblase.Simon R. BushellAshley C. W. PikeMaria E. FalzoneNils J. G. RorsmanChau M. TaRobin A. CoreyThomas D. NewportJohn C. ChristiansonLara F. ScofanoChitra A. ShintreAnnamaria TessitoreAmy ChuQinrui WangLeela ShresthaShubhashish M. M. MukhopadhyayJames D. LoveNicola A. Burgess-BrownRebecca SitsapesanPhillip J. StansfeldJuha T. HuiskonenPaolo TammaroAlessio AccardiElisabeth P. CarpenterNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Simon R. Bushell
Ashley C. W. Pike
Maria E. Falzone
Nils J. G. Rorsman
Chau M. Ta
Robin A. Corey
Thomas D. Newport
John C. Christianson
Lara F. Scofano
Chitra A. Shintre
Annamaria Tessitore
Amy Chu
Qinrui Wang
Leela Shrestha
Shubhashish M. M. Mukhopadhyay
James D. Love
Nicola A. Burgess-Brown
Rebecca Sitsapesan
Phillip J. Stansfeld
Juha T. Huiskonen
Paolo Tammaro
Alessio Accardi
Elisabeth P. Carpenter
The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K
description TMEM16K is a member of the TMEM16 family of integral membrane proteins that are either lipid scramblases or chloride channels. Here the authors combine cell biology, electrophysiology measurements, X-ray crystallography, cryo-EM and MD simulations to structurally characterize TMEM16K and show that it is an ER-resident lipid scramblase.
format article
author Simon R. Bushell
Ashley C. W. Pike
Maria E. Falzone
Nils J. G. Rorsman
Chau M. Ta
Robin A. Corey
Thomas D. Newport
John C. Christianson
Lara F. Scofano
Chitra A. Shintre
Annamaria Tessitore
Amy Chu
Qinrui Wang
Leela Shrestha
Shubhashish M. M. Mukhopadhyay
James D. Love
Nicola A. Burgess-Brown
Rebecca Sitsapesan
Phillip J. Stansfeld
Juha T. Huiskonen
Paolo Tammaro
Alessio Accardi
Elisabeth P. Carpenter
author_facet Simon R. Bushell
Ashley C. W. Pike
Maria E. Falzone
Nils J. G. Rorsman
Chau M. Ta
Robin A. Corey
Thomas D. Newport
John C. Christianson
Lara F. Scofano
Chitra A. Shintre
Annamaria Tessitore
Amy Chu
Qinrui Wang
Leela Shrestha
Shubhashish M. M. Mukhopadhyay
James D. Love
Nicola A. Burgess-Brown
Rebecca Sitsapesan
Phillip J. Stansfeld
Juha T. Huiskonen
Paolo Tammaro
Alessio Accardi
Elisabeth P. Carpenter
author_sort Simon R. Bushell
title The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K
title_short The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K
title_full The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K
title_fullStr The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K
title_full_unstemmed The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K
title_sort structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase tmem16k
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/602dd2cc133c49529d8807b7b0d875ca
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