Annexin A8 displays unique phospholipid and F-actin binding properties

FEBS Lett. 2006 May 1;580(10):2430-4. doi: 10.1016/j.febslet.2006.03.076. Epub 2006 Apr 7.


Annexin A8 is a poorly characterized member of the annexin family of Ca2+-regulated membrane binding proteins. Initially only identified at the cDNA level it had been tentatively linked to acute promyelocytic leukaemia (APL) due to its high and regulated expression in APL-derived cells. Here we identify unique properties of the annexin A8 protein. We show that it binds Ca2+-dependently and with high specificity to phosphatidylinositol (4,5)-bisphosphate (PtdIns(4,5)P2) and is also capable of interacting with F-actin. In line with these characteristics annexin A8 is recruited to F-actin-associated PtdIns(4,5)P2-rich membrane domains formed in HeLa cells upon infection with non-invading enteropathogenic Escherichia coli. These properties suggest a role of annexin A8 in the organization of certain actin-associated membrane domains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Annexins / metabolism*
  • Calcium / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • HeLa Cells
  • Humans
  • Phospholipids / metabolism*
  • Protein Binding


  • Actins
  • Annexins
  • Phospholipids
  • Calcium