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

Nat Commun. 2018 Oct 30;9(1):4511. doi: 10.1038/s41467-018-06990-9.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calmodulin-Binding Proteins / metabolism*
  • Cell Division / genetics
  • Centrioles / metabolism*
  • Centrosome / metabolism
  • Cilia / metabolism*
  • Cytoskeletal Proteins / metabolism*
  • Fibroblasts
  • HEK293 Cells
  • Humans
  • Mice
  • Mice, Knockout
  • Microtubule-Associated Proteins / metabolism*
  • Mitosis / genetics*
  • Phosphoproteins / genetics*
  • Phosphoproteins / metabolism
  • Protein Transport / genetics


  • CEP97 protein, mouse
  • Calmodulin-Binding Proteins
  • Cp110 protein, mouse
  • Cytoskeletal Proteins
  • Microtubule-Associated Proteins
  • Mphosph9 protein, human
  • Mphosph9 protein, mouse
  • Phosphoproteins