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Nature Cell Biology 1, E8 - E9 (1999)
doi:10.1038/8957

New twists for dynamin

Regis B. Kelly1

  1. Regis B. Kelly is in the Department of Biochemistry & Biophysics, Hormone Research Institute, University of California, San Francisco, San Francisco, California 94143-0534, USA.

Correspondence to: Regis B. Kelly1 e-mail: rkelly@biochem.ucsf.edu


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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