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Structural Studies of Dynamin Tubular Crystals by Cryo-Electron Microscopy

Published online by Cambridge University Press:  02 July 2020

Peijun Zhang  and
Jenny E. Hinshaw
Peijun Zhang
Affiliation:
Laboratory of Cell Biochemistry and Biology, NIDDK, NIH, Bethesda, MD20892, USA.
Jenny E. Hinshaw
Affiliation:
Laboratory of Cell Biochemistry and Biology, NIDDK, NIH, Bethesda, MD20892, USA.
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Extract

Dynamin is a 100 kD GTPase that plays an essential role in clathrin-coated vesicle formation during receptor mediated endocytosis, and in caveolae internalization and may play a role in intracellular membrane trafficking (1). It shares an extensive sequence homology (70% identity) to shibiregene product in Drosophila(2,3). The shibiretsmutants exhibit a rapid and reversible paralysis at non-permissive temperature due to a depletion of synaptic vesicles in their nerve termini which is believed to be caused by a block in endocytosis since there is an accumulation of “collared” clathrin-coated pits at the plasma membrane (4). Synaptosomes treated with GTPγs produces elongated necks surrounded by dynamin (6). Purified recombinant dynamin itself can assemble to form spirals and bind to lipid vesicles to form tubes, which resemble the “collar” at the necks of coated pits (5). These dynamin tubes vesiculate upon GTP treatment (7), suggesting a unique role of dynamin acting as a mechanoenzyme which causes clathrin-coated vesicles to be pinched off plasma membrane.

Type
Structural Approaches to the Study of Cell Cell Interactions In Three Dimensions
Information
Microscopy and Microanalysis , Volume 5 , Issue S2: Proceedings: Microscopy & Microanalysis '99, Microscopy Society of America 57th Annual Meeting, Microbeam Analysis Society 33rd Annual Meeting, Portland, Oregon August 1-5, 1999 , August 1999 , pp. 1024 - 1025
Copyright
Copyright © Microscopy Society of America

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References

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