期刊
FEBS LETTERS
卷 580, 期 10, 页码 2430-2434出版社
WILEY
DOI: 10.1016/j.febslet.2006.03.076
关键词
calcium; cytoskeleton; membrane binding; phosphoinositides
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)P-2) and is also capable of interacting with F-actin. In line with these characteristics annexin A8 is recruited to F-actin-associated Ptdlns(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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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