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The human kinetochore Ska1 complex facilitates microtubule depolymerization-coupled motility

Academic Article
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Overview

authors

  • Welburn, J. P. I.
  • Grishchuk, E. L.
  • Backer, C. B.
  • Wilson-Kubalek, Liz
  • Yates III, John
  • Cheeseman, I. M.

publication date

  • 2009

journal

  • Developmental Cell  Journal

abstract

  • Mitotic chromosome segregation requires that kinetochores attach to microtubule polymers and harness microtubule dynamics to drive chromosome movement. In budding yeast, the Dam1 complex couples kinetochores with microtubule depolymerization. However, a metazoan homolog of the Dam1 complex has not been identified. To identify proteins that play a corresponding role at the vertebrate kinetochore-microtubule interface, we isolated a three subunit human Ska1 complex, including the previously uncharacterized protein Rama1 that localizes to the outer kinetochore and spindle microtubules. Depletion of Ska1 complex subunits severely compromises proper chromosome segregation. Reconstituted Ska1 complex possesses two separable biochemical activities: direct microtubule binding through the Ska1 subunit, and microtubule-stimulated oligomerization imparted by the Rama1 subunit. The full Ska1 complex forms assemblies on microtubules that can facilitate the processive movement of microspheres along depolymerizing microtubules. In total, these results demonstrate a critical role for the Ska1 complex in interacting with dynamic microtubules at the outer kinetochore.

subject areas

  • Base Sequence
  • Cell Line
  • Chromosomal Proteins, Non-Histone
  • Chromosome Segregation
  • Fungal Proteins
  • Humans
  • Kinetochores
  • Microscopy, Electron, Transmission
  • Microspheres
  • Microtubule-Associated Proteins
  • Microtubules
  • Mitosis
  • Models, Biological
  • Movement
  • Multiprotein Complexes
  • Protein Binding
  • Protein Subunits
  • RNA, Small Interfering
  • Species Specificity
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Identity

PubMed Central ID

  • PMC2746561

International Standard Serial Number (ISSN)

  • 1534-5807

Digital Object Identifier (DOI)

  • 10.1016/j.devcel.2009.01.011

PubMed ID

  • 19289083
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Additional Document Info

start page

  • 374

end page

  • 385

volume

  • 16

issue

  • 3

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