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Published online March 26, 2007
doi:10.1083/jcb.200610072
The Journal of Cell Biology, Vol. 176, No. 7, 995-1005
The Rockefeller University Press, 0021-9525 $30.00
© 2007 White et al.
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Article

 Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing

Susan Roehl White1,2, Katia J. Evans1,2, Jeffrey Lary3, James L. Cole3,4, and Brett Lauring1,2

1 Department of Pathology and 2 Taub Institute, College of Physicians and Surgeons, Columbia University, New York, NY 10032
3 National Analytical Ultracentrifugation Facility and 4 Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269

Correspondence to Brett Lauring: bl320{at}columbia.edu

Spastin, an AAA ATPase mutated in the neurodegenerative disease hereditary spastic paraplegia, severs microtubules. Many other AAA proteins form ring-shaped hexamers and contain pore loops, which project into the ring's central cavity and act as ratchets that pull on target proteins, leading, in some cases, to conformational changes. We show that Spastin assembles into a hexamer and that loops within the central pore recognize C-terminal amino acids of tubulin. Key pore loop amino acids are required for severing, including one altered by a disease-associated mutation. We also show that Spastin contains a second microtubule binding domain that makes a distinct interaction with microtubules and is required for severing. Given that Spastin engages the MT in two places and that both interactions are required for severing, we propose that severing occurs by forces exerted on the C-terminal tail of tubulin, which results in a conformational change in tubulin, which releases it from the polymer.

Abbreviations used in this paper: EDC, ethyl-3-(dimethylaminopropyl)-carbodiimide; HSP, hereditary spastic paraplegia; MT, microtubule; MTBD, MT binding domain; WT, wild-type.


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