Annexin A8 displays unique phospholipid and F-actin binding properties.
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.
Goebeler
Verena
V
Institute for Medical Biochemistry, Centre for Molecular Biology of Inflammation, University of Münster, Von-Esmarch-Str. 56, D-48149 Münster, Germany.
Ruhe
Daniela
D
Gerke
Volker
V
Rescher
Ursula
U
D000199:Actins / Q000378:metabolism*; D017302:Annexins / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006367:HeLa Cells; D006801:Humans; D010743:Phospholipids / Q000378:metabolism*; D011485:Protein Binding
D000199:Actins; D017302:Annexins; D010743:Phospholipids; D002118:Calcium