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Putting a finger in the ring

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Two complementary papers demonstrate that the homologous type II transmembrane proteins LAP1 and LULL1 adopt nucleotide-free AAA+ ATPase folds and donate arginine fingers to complete the active sites of Torsin AAA+ ATPases. Activated Torsin complexes appear to function in nuclear and endoplasmic reticulum membrane-remodeling processes, including a nuclear vesiculation pathway that carries large cellular and viral cargoes from the nucleus into the cytoplasm.

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Figure 1: Arginine-finger interactions in small GTPases, AAA+ ATPases and the TorsinA–LAP1 complex.
Figure 2: Locations and interactions of Torsin complexes.

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Authors and Affiliations

  1. John McCullough and Wesley I. Sundquist are at the Department of Biochemistry, University of Utah, Salt Lake City, Utah, USA.,

    John McCullough & Wesley I Sundquist

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  1. John McCullough
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  2. Wesley I Sundquist
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Correspondence to Wesley I Sundquist.

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McCullough, J., Sundquist, W. Putting a finger in the ring. Nat Struct Mol Biol 21, 1025–1027 (2014). https://doi.org/10.1038/nsmb.2928

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