Kinesin-13s form rings around microtubules
Kinesin-13s form rings around microtubules
Kinesin is a superfamily of motor proteins that uses the energy of adenosine triphosphate hydrolysis to move and generate force along microtubules. A notable exception to this general description is found in the kinesin-13 family that actively depolymerizes microtubules rather than actively moving along them. This depolymerization activity is important in mitosis during chromosome segregation. It is still not fully clear by which mechanism kinesin-13s depolymerize microtubules. To address this issue, we used electron microscopy to investigate the interaction of kinesin-13s with microtubules. Surprisingly, we found that proteins of the kinesin-13 family form rings and spirals around microtubules. This is the first report of this type of oligomeric structure for any kinesin protein. These rings may allow kinesin-13s to stay at the ends of microtubules during depolymerization.
Adenosine Triphosphate/metabolism, Animals, Cricetinae, Drosophila/metabolism, Drosophila Proteins/chemistry, Kinesin/chemistry, Microtubules/chemistry, Models, Molecular, Molecular Conformation, Tubulin/chemistry
25-31
Tan, Dongyan
3b2a3d6f-8429-4901-b159-12c83f7d475b
Asenjo, Ana B
028f168e-5b2e-49fd-b0e2-84c48c4e9449
Mennella, Vito
43c60e29-c0a7-4ab8-8e5c-fcb59f70a28a
Sharp, David J
0e701ea9-7d32-4884-a57c-51b927c76ba3
Sosa, Hernando
0afbbc55-7dcf-4115-9620-0edfbc3d717f
9 October 2006
Tan, Dongyan
3b2a3d6f-8429-4901-b159-12c83f7d475b
Asenjo, Ana B
028f168e-5b2e-49fd-b0e2-84c48c4e9449
Mennella, Vito
43c60e29-c0a7-4ab8-8e5c-fcb59f70a28a
Sharp, David J
0e701ea9-7d32-4884-a57c-51b927c76ba3
Sosa, Hernando
0afbbc55-7dcf-4115-9620-0edfbc3d717f
Tan, Dongyan, Asenjo, Ana B, Mennella, Vito, Sharp, David J and Sosa, Hernando
(2006)
Kinesin-13s form rings around microtubules.
Journal of Cell Biology, 175 (1), .
(doi:10.1083/jcb.200605194).
Abstract
Kinesin is a superfamily of motor proteins that uses the energy of adenosine triphosphate hydrolysis to move and generate force along microtubules. A notable exception to this general description is found in the kinesin-13 family that actively depolymerizes microtubules rather than actively moving along them. This depolymerization activity is important in mitosis during chromosome segregation. It is still not fully clear by which mechanism kinesin-13s depolymerize microtubules. To address this issue, we used electron microscopy to investigate the interaction of kinesin-13s with microtubules. Surprisingly, we found that proteins of the kinesin-13 family form rings and spirals around microtubules. This is the first report of this type of oligomeric structure for any kinesin protein. These rings may allow kinesin-13s to stay at the ends of microtubules during depolymerization.
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More information
e-pub ahead of print date: 2 October 2006
Published date: 9 October 2006
Keywords:
Adenosine Triphosphate/metabolism, Animals, Cricetinae, Drosophila/metabolism, Drosophila Proteins/chemistry, Kinesin/chemistry, Microtubules/chemistry, Models, Molecular, Molecular Conformation, Tubulin/chemistry
Identifiers
Local EPrints ID: 434036
URI: http://eprints.soton.ac.uk/id/eprint/434036
ISSN: 0021-9525
PURE UUID: 948108f6-6ab4-4fab-a1ca-14df1527c8c8
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Date deposited: 11 Sep 2019 16:30
Last modified: 16 Mar 2024 04:04
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Author:
Dongyan Tan
Author:
Ana B Asenjo
Author:
David J Sharp
Author:
Hernando Sosa
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