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Protein kinase C regulates ErbB3 turnover.

Markus Dietrich1, Muhammad Salman Malik2, Marianne Skeie3

  • 1Department of Pathology, Oslo University Hospital, Oslo, Norway; Institute of Clinical Medicine, University of Oslo, Oslo, Norway.

Experimental Cell Research
|June 25, 2019
PubMed
Summary

Protein kinase C (PKC) regulates ErbB3 stability by altering its endosomal trafficking. Activated PKC stabilizes ErbB3, diverting it from degradation pathways, with PKCδ being crucial.

Keywords:
Endosomal sortingErbB3Phorbol 12-myristate 13-acetate (PMA)Protein kinase C (PKC)Receptor internalizationReceptor recycling

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Area of Science:

  • Cell biology
  • Molecular oncology
  • Signal transduction

Background:

  • ErbB3, a receptor tyrosine kinase, is implicated in human cancer progression.
  • ErbB protein regulation via endocytosis is critical; ErbB3 is constitutively internalized and degraded.
  • Protein kinase C (PKC) influences EGFR and ErbB2 stability and trafficking.

Purpose of the Study:

  • Investigate the effects of PKC activity on ErbB3 stability and intracellular trafficking.
  • Elucidate the role of PKC in the regulation of ErbB3 degradation and localization.

Main Methods:

  • Studied ErbB3 stability and trafficking in response to PKC activation and inhibition.
  • Utilized immunofluorescence microscopy to track ErbB3 localization in endosomal compartments (EEA1, LAMP1).
  • Performed knockdown experiments to identify specific PKC isoforms involved (PKCδ).

Main Results:

  • PKC activation stabilizes ErbB3, while PKC inhibition increases its degradation.
  • PKC activation reduces ErbB3 plasma membrane expression but does not inhibit internalization.
  • Activated PKC causes ErbB3 to localize in EEA1 and LAMP1-negative compartments, bypassing the degradative pathway.

Conclusions:

  • PKC regulates ErbB3 stability and intracellular trafficking.
  • PKCδ is essential for PKC-mediated regulation of ErbB3.
  • PKC activation likely redirects ErbB3 from the degradative pathway through altered endosomal sorting.