Annexin A8 displays unique phospholipid and F‐actin binding properties
Copyright policy )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.
- University of Münster Germany
Membrane binding, Annexins, Phosphoinositides, Actins, Humans, Calcium, Electrophoresis, Polyacrylamide Gel, Cytoskeleton, Phospholipids, HeLa Cells, Protein Binding
Membrane binding, Annexins, Phosphoinositides, Actins, Humans, Calcium, Electrophoresis, Polyacrylamide Gel, Cytoskeleton, Phospholipids, HeLa Cells, Protein Binding
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