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Mol Biol Cell. 2019 Aug 1;30(17):2097-2104. doi: 10.1091/mbc.E16-10-0709.

Open and cut: allosteric motion and membrane fission by dynamin superfamily proteins.

Kalia R1,2, Frost A3,2,4.

Author information

1
Department of Physiology, University of California, San Francisco, San Francisco, CA 94158.
2
Department of Biochemistry, University of Utah, Salt Lake City, UT 84132.
3
Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158.
4
Chan-Zuckerberg Biohub, San Francisco, CA 94158.

Abstract

Cells have evolved diverse protein-based machinery to reshape, cut, or fuse their membrane-delimited compartments. Dynamin superfamily proteins are principal components of this machinery and use their ability to hydrolyze GTP and to polymerize into helices and rings to achieve these goals. Nucleotide-binding, hydrolysis, and exchange reactions drive significant conformational changes across the dynamin family, and these changes alter the shape and stability of supramolecular dynamin oligomers, as well as the ability of dynamins to bind receptors and membranes. Mutations that interfere with the conformational repertoire of these enzymes, and hence with membrane fission, exist in several inherited human diseases. Here, we discuss insights from new x-ray crystal structures and cryo-EM reconstructions that have enabled us to infer some of the allosteric dynamics for these proteins. Together, these studies help us to understand how dynamins perform mechanical work, as well as how specific mutants of dynamin family proteins exhibit pathogenic properties.

PMID:
31365329
PMCID:
PMC6743466
[Available on 2019-10-16]
DOI:
10.1091/mbc.E16-10-0709

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