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The peptidyl-prolyl isomerase Pin1 regulates cytokinesis through Cep55

Armando van der Horst1, Kum Kum Khanna

  • 1Queensland Institute of Medical Research, Brisbane, Australia.

Cancer Research
|July 30, 2009
PubMed

Insights

The peptidyl-prolyl isomerase Pin1 regulates cell division (cytokinesis). Loss of Pin1 causes cell division defects, potentially contributing to cancer development by affecting genomic stability.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Biology

Background:

  • Cytokinesis failure leads to tetraploidy and genomic instability, common in cancer.
  • Pin1 (peptidyl-prolyl isomerase Pin1) is deregulated in tumors and controls cell cycle progression.

Purpose of the Study:

  • To investigate the role of Pin1 in cytokinesis.
  • To elucidate the mechanism by which Pin1 influences cytokinesis.

Main Methods:

  • Utilized Pin1 knockout mouse embryonic fibroblasts and Pin1-depleted HeLa cells.
  • Investigated Pin1 localization at the midbody ring.
  • Examined the interaction between Pin1 and centrosome protein 55 kDa (Cep55).
  • Assessed the impact of Pin1 on Cep55 phosphorylation by Polo-like kinase 1.

Main Results:

  • Pin1 knockout/depletion caused significant cytokinesis delays and defects.
  • Pin1 was found to localize to the midbody ring and bind to Cep55.
  • Pin1 facilitates Polo-like kinase 1-mediated phosphorylation of Cep55, crucial for its function.
  • Pin1 and Cep55 function within the same pathway, as Pin1 knockdown did not worsen Cep55 depletion-induced defects.

Conclusions:

  • Pin1 plays a novel and critical role in regulating the final stages of cytokinesis.
  • The Pin1-Cep55 interaction and subsequent Cep55 phosphorylation are key mechanisms.
  • Pathologic Pin1 levels may contribute to tumorigenesis through cytokinesis disruption and genomic instability.

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