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

Ning Huang, Donghui Zhang, Fangyuan Li, Peiyuan Chai, Song Wang, Junlin Teng () and Jianguo Chen ()
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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

Nature Communications, 2018, vol. 9, issue 1, 1-15

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-06990-9

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