Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Orientation and structure of the Ndc80 complex on the microtubule lattice

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

related to degree

  • Yoshioka, Craig, Ph.D. in Biophysics, Scripps Research 2003 - 2008

authors

  • Wilson-Kubalek, Liz
  • Cheeseman, I. M.
  • Yoshioka, Craig
  • Desai, A.
  • Milligan, Ronald

publication date

  • September 2008

journal

  • Journal of Cell Biology  Journal

abstract

  • The four-subunit Ndc80 complex, comprised of Ndc80/Nuf2 and Spc24/Spc25 dimers, directly connects kinetochores to spindle microtubules. The complex is anchored to the kinetochore at the Spc24/25 end, and the Ndc80/Nuf2 dimer projects outward to bind to microtubules. Here, we use cryoelectron microscopy and helical image analysis to visualize the interaction of the Ndc80/Nuf2 dimer with microtubules. Our results, when combined with crystallography data, suggest that the globular domain of the Ndc80 subunit binds strongly at the interface between tubulin dimers and weakly at the adjacent intradimer interface along the protofilament axis. Such a binding mode, in which the Ndc80 complex interacts with sequential alpha/beta-tubulin heterodimers, may be important for stabilizing kinetochore-bound microtubules. Additionally, we define the binding of the Ndc80 complex relative to microtubule polarity, which reveals that the microtubule interaction surface is at a considerable distance from the opposite kinetochore-anchored end; this binding geometry may facilitate polymerization and depolymerization at kinetochore-attached microtubule ends.

subject areas

  • Cell Cycle Proteins
  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Dimerization
  • Humans
  • Kinetochores
  • Microtubules
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Proteins
  • Protein Conformation
  • Protein Subunits
  • Spindle Apparatus
scroll to property group menus

Identity

PubMed Central ID

  • PMC2542468

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200804170

PubMed ID

  • 18794333
scroll to property group menus

Additional Document Info

start page

  • 1055

end page

  • 1061

volume

  • 182

issue

  • 6

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support