AHNAK interaction with the annexin 2/S100A10 complex regulates cell membrane cytoarchitecture

  • Benaud C
  • Gentil B
  • Assard N
 et al. 
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Remodelling of the plasma membrane cytoarchitecture is crucial for the regulation of epithelial cell adhesion and permeability. In Madin-Darby canine kidney cells, the protein AHNAK relocates from the cytosol to the cytosolic surface of the plasma membrane during the formation of cell-cell contacts and the development of epithelial polarity. This targeting is reversible and regulated by Ca2+-dependent cell-cell adhesion. At the plasma membrane, AHNAK associates as a multimeric complex with actin and the annexin 2/S100A10 complex. The S100A10 subunit serves to mediate the interaction between annexin 2 and the COOH-terminal regulatory domain of AHNAK. Down-regulation of both annexin 2 and S100A10 using an annexin 2-specific small interfering RNA inhibits the association of AHNAK with plasma membrane. In Madin-Darby canine kidney cells, down-regulation of AHNAK using AHNAK-specific small interfering RNA prevents cortical actin cytoskeleton reorganization required to support cell height. We propose that the interaction of AHNAK with the annexin 2/S100A10 regulates cortical actin cytoskeleton organization and cell membrane cytoarchitecture.

Author-supplied keywords

  • Actin
  • Calcium
  • Cell adhesion
  • Cytoskeleton
  • S100B

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  • Christelle Benaud

  • Benoît J. Gentil

  • Nicole Assard

  • Magalie Court

  • Jerome Garin

  • Christian Delphin

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