Complex formation and submembranous localization of annexin 2 and S100A10 in live HepG2 cells

FEBS Lett. 2001 Jul 6;500(3):137-40. doi: 10.1016/s0014-5793(01)02604-7.

Abstract

The Ca(2+) and membrane binding protein annexin 2 can form a heterotetrameric complex with the S100A10 protein and this complex is thought to serve a bridging or scaffolding function in the membrane underlying cytoskeleton. To elucidate which of the subunits targets the complex to the subplasmalemmal region in live cells we employed YFP/CFP fusion proteins and live cell imaging in HepG2 cells. We show that monomeric annexin 2 is targeted to the plasma membrane whereas non-complexed S100A10 acquires a general cytosolic distribution. Co-expression of S100A10 together with annexin 2 and the resulting complex formation, however, lead to a recruitment of S100A10 to the plasma membrane thus identifying annexin 2 as the membrane targeting subunit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Annexin A2 / genetics
  • Annexin A2 / metabolism*
  • Calcium-Binding Proteins / genetics
  • Calcium-Binding Proteins / metabolism*
  • Carcinoma, Hepatocellular / metabolism*
  • Carcinoma, Hepatocellular / ultrastructure
  • Cell Membrane / metabolism*
  • Cell Membrane / ultrastructure
  • Cytoskeleton / metabolism
  • Cytosol / metabolism
  • Humans
  • Luminescent Proteins / genetics
  • Macromolecular Substances
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • S100 Proteins*
  • Tumor Cells, Cultured

Substances

  • Annexin A2
  • Calcium-Binding Proteins
  • Luminescent Proteins
  • Macromolecular Substances
  • Recombinant Fusion Proteins
  • S100 Proteins
  • S100 calcium binding protein A10