The AAA+ ATPase TRIP13 remodels HORMA domains through N-terminal engagement and unfolding.

@article{Ye2017TheAA,
  title={The AAA+ ATPase TRIP13 remodels HORMA domains through N-terminal engagement and unfolding.},
  author={Qiaozhen Ye and Dong Hyun Kim and Ihsan Dereli and Scott C. Rosenberg and Goetz Hagemann and Franz Herzog and A. Hargitaine Toth and Don W Cleveland and Kevin D Corbett},
  journal={The EMBO journal},
  year={2017},
  volume={36 16},
  pages={
          2419-2434
        }
}
Proteins of the conserved HORMA domain family, including the spindle assembly checkpoint protein MAD2 and the meiotic HORMADs, assemble into signaling complexes by binding short peptides termed "closure motifs". The AAA+ ATPase TRIP13 regulates both MAD2 and meiotic HORMADs by disassembling these HORMA domain-closure motif complexes, but its mechanisms of substrate recognition and remodeling are unknown. Here, we combine X-ray crystallography and crosslinking mass spectrometry to outline how… CONTINUE READING
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