Structural basis for the activation of the lipid scramblase TMEM16F

Melanie Arndt; Carolina Alvadia; Monique S. Straub; Vanessa Clerico Mosina; Cristina Paulino; Raimund Dutzler

doi:10.1038/s41467-022-34497-x

Nature Communications (Nov 2022)

Structural basis for the activation of the lipid scramblase TMEM16F

Melanie Arndt,
Carolina Alvadia,
Monique S. Straub,
Vanessa Clerico Mosina,
Cristina Paulino,
Raimund Dutzler

Affiliations

Melanie Arndt: Department of Biochemistry University of Zurich
Carolina Alvadia: Department of Biochemistry University of Zurich
Monique S. Straub: Department of Biochemistry University of Zurich
Vanessa Clerico Mosina: Department of Structural Biology and Membrane Enzymology at the Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen
Cristina Paulino: Department of Structural Biology and Membrane Enzymology at the Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen
Raimund Dutzler: Department of Biochemistry University of Zurich

DOI: https://doi.org/10.1038/s41467-022-34497-x
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 17

Abstract

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TMEM16F is a dual ion channel and lipid scramblase that is involved in blood coagulation and cell fusion. Here, authors elucidate how the protein is activated by Ca2+ to accomplish both functions in a single protein conformation.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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