We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Annexin A8 displays unique phospholipid and F-actin binding properties
- Authors
Goebeler, Verena; Ruhe, Daniela; Gerke, Volker; Rescher, Ursula
- Abstract
Abstract: 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.
- Subjects
ACTIN; CLONE cells; CANCER cells; ESCHERICHIA coli
- Publication
FEBS Letters, 2006, Vol 580, Issue 10, p2430
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2006.03.076