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Self-Assembly of Dynamin

Published online by Cambridge University Press:  02 July 2020

Dganit Danino
Affiliation:
National Institute of Health, Bethesda, MD
Jenny E. Hinshaw
Affiliation:
National Institute of Health, Bethesda, MD

Abstract

Dynamin is a large GTPase essential for various intracellular processes such as synaptic vesicle recycling, caveolae internalization and trafficking into and out of the Golgi. It is also involved in receptor-mediated endocytosis, and is believed to assemble at the necks of clathrin-coated pits and assist in pinching vesicles from the plasma membrane upon GTP binding and hydrolysis.

Purified recombinant dynamin self-assembles into rings and spirals in low salt conditions [1]. A dynamin mutant lacking the c-terminal proline rich domain (APRD) also assembles into rings and spirals, however unlike wild type dynamin APRD constricts in the presence of GTP analogous such as GMP-PCP [2] or GTPγS. to explore differences in the behavior of the wild type and mutant dynamin we dialyzed them into different salt solutions containing various types of nucleotides and studied their assembly over time using negative staining and cryo-TEM.

Type
Recent Techniques for the Fixation and Staining of Biological Samples (Organized by M. Sanders and K. McDonald)
Copyright
Copyright © Microscopy Society of America 2001

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References

1.Hinshaw, JE and SL, Schmid, Nature 374. 190-2 (1995).CrossRefGoogle Scholar
2.Zhang, P and Hinshaw, EJ, (manuscript submitted).Google Scholar
3.Carr, JF and Hinshaw, EJ,.J. Biol. Chem. 272. 28030-35 (1997).CrossRefGoogle Scholar

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