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New twists for dynamin

Nature Cell Biology volume 1, pages E8–E9 (1999)Cite this article

Abstract

New in vitro and mutagenesis studies of dynamin, a protein involved in the process of vesicle internalization from the plasma membrane, suggest either a "poppase" or a regulatory mechanism for dynamin action, and illustrate the importance of dynamin-binding partners.

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Figure 1: Domains of dynamin.
Figure 2: The three experimental systems used to study dynamin twists.

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Authors and Affiliations

  1. Department of Biochemistry & Biophysics, Hormone Research Institute, University of California, San Francisco, San Francisco, 94143-0534, California, USA

    Regis B. Kelly

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  1. Regis B. Kelly
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Correspondence to Regis B. Kelly.

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Kelly, R. New twists for dynamin. Nat Cell Biol 1, E8–E9 (1999). https://doi.org/10.1038/8957

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