Nature Communications (Sep 2019)
The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K
- 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
Affiliations
- Simon R. Bushell
- Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford
- Ashley C. W. Pike
- Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford
- Maria E. Falzone
- Department of Biochemistry, Weill Cornell Medical School
- Nils J. G. Rorsman
- Department of Pharmacology, University of Oxford
- Chau M. Ta
- Department of Pharmacology, University of Oxford
- Robin A. Corey
- Department of Biochemistry, University of Oxford
- Thomas D. Newport
- Department of Biochemistry, University of Oxford
- John C. Christianson
- Nuffield Department of Rheumatology, Orthopaedics and Musculoskeletal Sciences, University of Oxford
- Lara F. Scofano
- Department of Pharmacology, University of Oxford
- Chitra A. Shintre
- Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford
- Annamaria Tessitore
- Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford
- Amy Chu
- Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford
- Qinrui Wang
- Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford
- Leela Shrestha
- Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford
- Shubhashish M. M. Mukhopadhyay
- Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford
- James D. Love
- Department of Biochemistry, Albert Einstein College of Medicine
- Nicola A. Burgess-Brown
- Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford
- Rebecca Sitsapesan
- Department of Pharmacology, University of Oxford
- Phillip J. Stansfeld
- Department of Biochemistry, University of Oxford
- Juha T. Huiskonen
- Division of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford
- Paolo Tammaro
- Department of Pharmacology, University of Oxford
- Alessio Accardi
- Department of Biochemistry, Weill Cornell Medical School
- Elisabeth P. Carpenter
- Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford
- DOI
- https://doi.org/10.1038/s41467-019-11753-1
- Journal volume & issue
-
Vol. 10,
no. 1
pp. 1 – 16
Abstract
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.
