Insights into EB1 structure and the role of its C-terminal domain for discriminating microtubule tips from the lattice

@inproceedings{Buey2011InsightsIE,
  title={Insights into EB1 structure and the role of its C-terminal domain for discriminating microtubule tips from the lattice},
  author={Rub{\'e}n M Buey and Renu Mohan and Kris Leslie and Thomas Walzthoeni and John H. Missimer and Andreas Menzel and Sa{\vs}a Bjeli{\'c} and Katja Bargsten and Ilya Grigoriev and Ihor Smal and Erik H. W. Meijering and Ruedi Aebersold and Anna Akhmanova and Michel O. Steinmetz},
  booktitle={Molecular biology of the cell},
  year={2011}
}
End-binding proteins (EBs) comprise a conserved family of microtubule plus end-tracking proteins. The concerted action of calponin homology (CH), linker, and C-terminal domains of EBs is important for their autonomous microtubule tip tracking, regulation of microtubule dynamics, and recruitment of numerous partners to microtubule ends. Here we report the detailed structural and biochemical analysis of mammalian EBs. Small-angle X-ray scattering, electron microscopy, and chemical cross-linking… CONTINUE READING

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