Traffic. 2000 May;1(5):385-92.

Garrotes, springs, ratchets, and whips: putting dynamin models to the test.

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Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and Dana Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, USA.

Abstract

The GTPase dynamin is essential for clathrin-mediated endocytosis. Numerous new and exciting discoveries regarding dynamin function in vivo and in vitro have led to various models in which dynamin functions directly in membrane fission and the release of clathrin-coated vesicles from the plasma membrane. This would make dynamin unique among GTPases in its ability to act as a mechanochemical enzyme. Here we review the various models and their supporting data. We then discuss new findings that raise doubts as to whether dynamin breaks the paradigm that governs regulatory GTPases.

PMID:: 11208124; [PubMed - indexed for MEDLINE]

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Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring. [Nat Cell Biol. 1999]
Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring.
Stowell MH, Marks B, Wigge P, McMahon HT. Nat Cell Biol. 1999 May; 1(1):27-32.
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Review Dynamin GTPase, a force-generating molecular switch. [Bioessays. 1996]
Review Dynamin GTPase, a force-generating molecular switch.
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Fabrikant G, Lata S, Riches JD, Briggs JA, Weissenhorn W, Kozlov MM. PLoS Comput Biol. 2009 Nov; 5(11):e1000575. Epub 2009 Nov 20.
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Garrotes, springs, ratchets, and whips: putting dynamin models to the test.
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Garrotes, springs, ratchets, and whips: putting dynamin models to the test.

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