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Annexin A8 displays unique phospholipid and F‐actin binding properties
Author(s) -
Goebeler Verena,
Ruhe Daniela,
Gerke Volker,
Rescher Ursula
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.076
Subject(s) - annexin a2 , annexin , phosphatidylinositol , actin , microbiology and biotechnology , hela , annexin a1 , chemistry , biology , biochemistry , cell , signal transduction
Annexin A8 is a poorly characterized member of the annexin family of Ca 2+ ‐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 Ca 2+ ‐dependently and with high specificity to phosphatidylinositol (4,5)‐bisphosphate (PtdIns(4,5)P 2 ) 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)P 2 ‐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.