The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn

F. Esra Demircioglu; Weili Zheng; Alexander J. McQuown; Nolan K. Maier; Nicki Watson; Iain M. Cheeseman; Vladimir Denic; Edward H. Egelman; Thomas U. Schwartz

doi:10.1038/s41467-019-11194-w

Nature Communications (Jul 2019)

The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn

F. Esra Demircioglu,
Weili Zheng,
Alexander J. McQuown,
Nolan K. Maier,
Nicki Watson,
Iain M. Cheeseman,
Vladimir Denic,
Edward H. Egelman,
Thomas U. Schwartz

Affiliations

F. Esra Demircioglu: Department of Biology, Massachusetts Institute of Technology
Weili Zheng: Department of Biochemistry and Molecular Genetics, University of Virginia
Alexander J. McQuown: Department of Molecular and Cellular Biology, Harvard University
Nolan K. Maier: Department of Biology, Massachusetts Institute of Technology
Nicki Watson: W. M. Keck Microscopy Facility, The Whitehead Institute
Iain M. Cheeseman: Department of Biology, Massachusetts Institute of Technology
Vladimir Denic: Department of Molecular and Cellular Biology, Harvard University
Edward H. Egelman: Department of Biochemistry and Molecular Genetics, University of Virginia
Thomas U. Schwartz: Department of Biology, Massachusetts Institute of Technology

DOI: https://doi.org/10.1038/s41467-019-11194-w
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 12

Abstract

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Torsins are unusual AAA + ATPases of unknown function that reside in the endoplasmic reticulum of all animals. Here the authors report that TorsinA forms tubular helical filaments with an unusual periodicity and that filamentous TorsinA directly interacts with membranes to form tubular protrusions.

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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