Novel septin 9 repeat motifs altered in neuralgic amyotrophy bind and bundle microtubules

@inproceedings{Bai2013NovelS9,
  title={Novel septin 9 repeat motifs altered in neuralgic amyotrophy bind and bundle microtubules},
  author={Xiaobo Bai and Jonathan R. Bowen and Tara K. Knox and Kaifeng Zhou and Manuela Pendziwiat and Gregor Kuhlenb{\"a}umer and Charles Vaughn Sindelar and Elias T Spiliotis},
  booktitle={The Journal of cell biology},
  year={2013}
}
Septin 9 (SEPT9) interacts with microtubules (MTs) and is mutated in hereditary neuralgic amyotrophy (HNA), an autosomal-dominant neuropathy. The mechanism of SEPT9 interaction with MTs and the molecular basis of HNA are unknown. Here, we show that the N-terminal domain of SEPT9 contains the novel repeat motifs K/R-x-x-E/D and R/K-R-x-E, which bind and bundle MTs by interacting with the acidic C-terminal tails of β-tubulin. Alanine scanning mutagenesis revealed that the K/R-R/x-x-E/D motifs… CONTINUE READING
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