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Cep97 and CP110 suppress a cilia assembly program.

Mammalian centrioles play a dynamic role in centrosome function, but they also have the capacity to nucleate the assembly of cilia. Although controls must exist to specify these different fates, the key regulators remain largely undefined. We have purified complexes associated with CP110, a protein that plays an essential role in centrosome duplication and cytokinesis, and have identified a previously uncharacterized protein, Cep97, that recruits CP110 to centrosomes. Depletion of Cep97 or expression of dominant-negative mutants results in CP110 disappearance from centrosomes, spindle defects, and polyploidy. Remarkably, loss of Cep97 or CP110 promotes primary cilia formation in growing cells, and enforced expression of CP110 in quiescent cells suppresses their ability to assemble cilia, suggesting that Cep97 and CP110 collaborate to inhibit a ciliogenesis program. Identification of Cep97 and other genes involved in regulation of cilia assembly may accelerate our understanding of human ciliary diseases, including renal disease and retinal degeneration.

Pubmed ID: 17719545

Authors

  • Spektor A
  • Tsang WY
  • Khoo D
  • Dynlacht BD

Journal

Cell

Publication Data

August 24, 2007

Associated Grants

  • Agency: NIGMS NIH HHS, Id: T32 GM007308

Mesh Terms

  • Animals
  • Cell Cycle Proteins
  • Cell Line
  • Cell Line, Tumor
  • Centrioles
  • Centrosome
  • Cilia
  • Cytokinesis
  • Green Fluorescent Proteins
  • Humans
  • Kidney
  • Mice
  • Microtubule-Associated Proteins
  • Models, Biological
  • Mutation
  • NIH 3T3 Cells
  • Phosphoproteins
  • Polyploidy
  • Precipitin Tests
  • RNA Interference
  • RNA, Small Interfering
  • Recombinant Fusion Proteins
  • Spindle Apparatus