Skip to main content Accessibility help
×
Home
Hostname: page-component-768ffcd9cc-727vs Total loading time: 0.256 Render date: 2022-12-07T07:34:47.549Z Has data issue: true Feature Flags: { "useRatesEcommerce": false } hasContentIssue true

Structural Studies of Dynamin Tubular Crystals by Cryo-Electron Microscopy

Published online by Cambridge University Press:  02 July 2020

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.

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
Copyright
Copyright © Microscopy Society of America

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1. Schmid, S. L., McNiven, M. A. & De Camilli, P.Curr Opin Cell Biol 10, 504512 (1998).CrossRefGoogle Scholar

2. van der Bliek, A. M., & Meyerowitz, E. M.Nature 351, 411414 (1991).CrossRefGoogle Scholar

3. Chen, M. S., et al. Nature 351, 583586 (1991).CrossRefGoogle Scholar

4. Koenig, J. H., & Ikeda, K.J Neurosci 9, 38443860 (1989).CrossRefGoogle Scholar

5. Hinshaw, J. E., & Schmid, S. L.Nature 374, 190192 (1995).CrossRefGoogle Scholar

6. Takei, K., et al. Nature 374, 186190 (1995).CrossRefGoogle Scholar

7. Sweitzer, S. M. and Hinshaw, J. E.Cell 93, 1021-1029(1998)CrossRefGoogle Scholar

Save article to Kindle

To save this article to your Kindle, first ensure coreplatform@cambridge.org is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about saving to your Kindle.

Note you can select to save to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be saved to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

Find out more about the Kindle Personal Document Service.

Structural Studies of Dynamin Tubular Crystals by Cryo-Electron Microscopy
Available formats
×

Save article to Dropbox

To save this article to your Dropbox account, please select one or more formats and confirm that you agree to abide by our usage policies. If this is the first time you used this feature, you will be asked to authorise Cambridge Core to connect with your Dropbox account. Find out more about saving content to Dropbox.

Structural Studies of Dynamin Tubular Crystals by Cryo-Electron Microscopy
Available formats
×

Save article to Google Drive

To save this article to your Google Drive account, please select one or more formats and confirm that you agree to abide by our usage policies. If this is the first time you used this feature, you will be asked to authorise Cambridge Core to connect with your Google Drive account. Find out more about saving content to Google Drive.

Structural Studies of Dynamin Tubular Crystals by Cryo-Electron Microscopy
Available formats
×
×

Reply to: Submit a response

Please enter your response.

Your details

Please enter a valid email address.

Conflicting interests

Do you have any conflicting interests? *