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M-Phase Phosphoprotein 9 regulates ciliogenesis by modulating CP110-CEP97 complex localization at the mother centriole

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Listed:
  • Ning Huang

    (Peking University)

  • Donghui Zhang

    (Peking University)

  • Fangyuan Li

    (Peking University)

  • Peiyuan Chai

    (Peking University)

  • Song Wang

    (Peking University)

  • Junlin Teng

    (Peking University)

  • Jianguo Chen

    (Peking University
    Peking University)

Abstract

The primary cilium is elongated from the mother centriole and has diverse signaling roles during development and disease. The CP110-CEP97 complex functions as a negative regulator of ciliogenesis, although the mechanisms regulating its mother centriole localization are poorly understood. Here we show that M-Phase Phosphoprotein 9 (MPP9) is recruited by Kinesin Family Member 24 (KIF24) to the distal end of mother centriole where it forms a ring-like structure and recruits CP110-CEP97 by directly binding CEP97. Loss of MPP9 causes abnormal primary cilia formation in growing cells and mouse kidneys. After phosphorylation by Tau Tubulin Kinase 2 (TTBK2) at the beginning of ciliogenesis, MPP9 is targeted for degradation via the ubiquitin-proteasome system, which facilitates the removal of CP110 and CEP97 from the distal end of the mother centriole. Thus, MPP9 acts as a regulator of ciliogenesis by regulating the localization of CP110-CEP97 at the mother centriole.

Suggested Citation

  • Ning Huang & Donghui Zhang & Fangyuan Li & Peiyuan Chai & Song Wang & Junlin Teng & Jianguo Chen, 2018. "M-Phase Phosphoprotein 9 regulates ciliogenesis by modulating CP110-CEP97 complex localization at the mother centriole," Nature Communications, Nature, vol. 9(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06990-9
    DOI: 10.1038/s41467-018-06990-9
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