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G domain dimerization controls dynamin's assembly-stimulated GTPase activity

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  • Joshua S. Chappie

    (Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, Maryland 20892, USA
    The Scripps Research Institute, La Jolla, California 92037, USA)

  • Sharmistha Acharya

    (The Scripps Research Institute, La Jolla, California 92037, USA)

  • Marilyn Leonard

    (The Scripps Research Institute, La Jolla, California 92037, USA)

  • Sandra L. Schmid

    (The Scripps Research Institute, La Jolla, California 92037, USA)

  • Fred Dyda

    (Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, Maryland 20892, USA)

Abstract

Dynamin is an atypical GTPase that catalyses membrane fission during clathrin-mediated endocytosis. The mechanisms of dynamin’s basal and assembly-stimulated GTP hydrolysis are unknown, though both are indirectly influenced by the GTPase effector domain (GED). Here we present the 2.0 Å resolution crystal structure of a human dynamin 1-derived minimal GTPase–GED fusion protein, which was dimeric in the presence of the transition state mimic GDP.AlF4-.The structure reveals dynamin’s catalytic machinery and explains how assembly-stimulated GTP hydrolysis is achieved through G domain dimerization. A sodium ion present in the active site suggests that dynamin uses a cation to compensate for the developing negative charge in the transition state in the absence of an arginine finger. Structural comparison to the rat dynamin G domain reveals key conformational changes that promote G domain dimerization and stimulated hydrolysis. The structure of the GTPase–GED fusion protein dimer provides insight into the mechanisms underlying dynamin-catalysed membrane fission.

Suggested Citation

  • Joshua S. Chappie & Sharmistha Acharya & Marilyn Leonard & Sandra L. Schmid & Fred Dyda, 2010. "G domain dimerization controls dynamin's assembly-stimulated GTPase activity," Nature, Nature, vol. 465(7297), pages 435-440, May.
    • Handle: RePEc:nat:nature:v:465:y:2010:i:7297:d:10.1038_nature09032
    DOI: 10.1038/nature09032
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    Cited by:

    1. Katherine Bonnycastle & Katharine L. Dobson & Eva-Maria Blumrich & Akshada Gajbhiye & Elizabeth C. Davenport & Marie Pronot & Moritz Steinruecke & Matthias Trost & Alfredo Gonzalez-Sulser & Michael A., 2023. "Reversal of cell, circuit and seizure phenotypes in a mouse model of DNM1 epileptic encephalopathy," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    2. Lucas Gewehr & Benedikt Junglas & Ruven Jilly & Johannes Franz & Wenyu Eva Zhu & Tobias Weidner & Mischa Bonn & Carsten Sachse & Dirk Schneider, 2023. "SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

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