Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin

Antonina Roll-Mecak and Ronald D. Vale ()
Additional contact information
Antonina Roll-Mecak: University of California, San Francisco, 600 16th Street, San Francisco, California 94158, USA
Ronald D. Vale: University of California, San Francisco, 600 16th Street, San Francisco, California 94158, USA

Nature, 2008, vol. 451, issue 7176, 363-367

Abstract: Spastin structure revealed Spastin, a microtubule severing protein involved in the assembly or function of nuclear protein complexes, has attracted interest because of its role in neuronal synapse formation, and the discovery that mutations in the gene cause hereditary neurodegenerative disease. The structure of spastin has now been determined to atomic resolution by X-ray crystallography, revealing an AAA ATPase cassette augmented by structural elements unique to the microtubule severing enzyme subfamily. Mapping of hereditary spastic paraplegia mutations onto the structure of spastin reveals how disease mutations damage the enzyme.

Date: 2008
References: Add references at CitEc
Citations: View citations in EconPapers (3)

Downloads: (external link)
https://www.nature.com/articles/nature06482 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:451:y:2008:i:7176:d:10.1038_nature06482

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature06482

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().