CENP-T provides a structural platform for outer kinetochore assembly.

@article{Nishino2013CENPTPA,
  title={CENP-T provides a structural platform for outer kinetochore assembly.},
  author={Tatsuya Nishino and Florencia Rago and Tetsuya Hori and Kentaro Tomii and Iain M Cheeseman and Tatsuo Fukagawa},
  journal={The EMBO journal},
  year={2013},
  volume={32 3},
  pages={424-36}
}
The kinetochore forms a dynamic interface with microtubules from the mitotic spindle during mitosis. The Ndc80 complex acts as the key microtubule-binding complex at kinetochores. However, it is unclear how the Ndc80 complex associates with the inner kinetochore proteins that assemble upon centromeric chromatin. Here, based on a high-resolution structural analysis, we demonstrate that the N-terminal region of vertebrate CENP-T interacts with the 'RWD' domain in the Spc24/25 portion of the Ndc80… CONTINUE READING
Related Discussions
This paper has been referenced on Twitter 1 time. VIEW TWEETS

Citations

Publications citing this paper.
Showing 1-10 of 71 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 50 references

The MORPHEUS protein crystallization screen

Journal of applied crystallography • 2009
View 4 Excerpts
Highly Influenced

Structural organization of the kinetochore-microtubule interface.

Current opinion in cell biology • 2012
View 4 Excerpts
Highly Influenced

Towards rationalization of crystallization screening for small- to medium-sized academic laboratories: the PACT/JCSG+ strategy.

Acta crystallographica. Section D, Biological crystallography • 2005
View 2 Excerpts
Highly Influenced

A mechanism for the evolution of phosphorylation sites

SM Pearlman, Z Serber
Cell • 2011

Similar Papers

Loading similar papers…