Annexin A8 displays unique phospholipid and F-actin binding properties.
FEBS Lett
; 580(10): 2430-4, 2006 May 01.
Article
en En
| MEDLINE
| ID: mdl-16638567
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.
Buscar en Google
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Fosfolípidos
/
Actinas
/
Anexinas
Límite:
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
2006
Tipo del documento:
Article
País de afiliación:
Alemania