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Dap160/intersectin binds and activates aPKC to regulate cell polarity and cell cycle progression

Chiswili Chabu1, Chris Q Doe

  • 1Institute of Neuroscience, Institute of Molecular Biology, Howard Hughes Medical Institute, University of Oregon, Eugene, OR 97403, USA.

Development (Cambridge, England)
|July 11, 2008
PubMed

Insights

Dynamin-associated protein 160 (Dap160) regulates atypical protein kinase C (aPKC) activity and localization. This interaction is crucial for neuroblast cell polarity and cell cycle progression in Drosophila.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Developmental Biology

Background:

  • Atypical protein kinase C (aPKC) is vital for cell polarization and growth control.
  • aPKC dysregulation is implicated in human tumor development.
  • Mechanisms regulating aPKC activity remain largely uncharacterized.

Purpose of the Study:

  • To identify novel regulators of aPKC.
  • To elucidate the role of aPKC in neuroblast cell polarity and proliferation.

Main Methods:

  • Biochemical assays to identify interacting proteins.
  • In vitro kinase assays to measure aPKC activity.
  • Immunofluorescence microscopy to determine protein localization.
  • Analysis of mutant phenotypes in Drosophila neuroblasts.

Main Results:

  • Dap160 directly interacts with aPKC and enhances its kinase activity in vitro.
  • Dap160 colocalizes with aPKC at the apical cortex of neuroblasts.
  • Loss of Dap160 leads to aPKC delocalization and reduced activity.
  • Mutations in dap160 or aPKC result in fewer proliferating neuroblasts and extended cell cycles.

Conclusions:

  • Dap160 acts as a positive regulator of aPKC.
  • Dap160 is essential for proper aPKC localization and function.
  • Dap160-aPKC pathway is critical for neuroblast cell polarity and cell cycle progression.

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