Kinesin-13s form rings around microtubules

Dongyan Tan, Ana B. Asenjo, Vito Mennella, David J. Sharp, Hernando Sosa

Research output: Contribution to journalArticlepeer-review

45 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)25-31
Number of pages7
JournalJournal of Cell Biology
Volume175
Issue number1
DOIs
StatePublished - Oct 9 2006

ASJC Scopus subject areas

  • Cell Biology

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