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Annexin A6 is an organizer of membrane microdomains to regulate receptor localization and signalling
Author(s) -
Cornely Rhea,
Rentero Carles,
Enrich Carlos,
Grewal Thomas,
Gaus Katharina
Publication year - 2011
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.540
Subject(s) - microbiology and biotechnology , lipid raft , annexin a2 , annexin , actin cytoskeleton , cytoskeleton , endosome , lipid microdomain , cell membrane , receptor , actin , cell surface receptor , chemistry , cell , biology , membrane , signal transduction , biochemistry , intracellular
Annexin A6 (AnxA6) belongs to the conserved annexin protein family—a group of Ca 2+ ‐dependent membrane binding proteins. It is the largest of all annexin proteins and upon activation, binds to negatively charged phospholipids in the plasma membrane and endosomes. In addition, AnxA6 associates with cholesterol‐rich membrane microdomains termed lipid rafts. Membrane cholesterol triggers Ca 2+ ‐independent translocation of AnxA6 to membranes and AnxA6 levels determine the number of caveolae, a form of specialized rafts at the cell surface. AnxA6 also has an F‐actin binding domain and interacts with cytoskeleton components. Taken together, this suggests that AnxA6 has a scaffold function to link membrane microdomains with the organization of the cytoskeleton. Such a link facilitates AnxA6 to participate in plasma membrane repair and it would also impact on receptor signalling at the cell surface, growth factor, and lipoprotein receptor trafficking, Ca 2+ ‐channel activity and T cell activation. Hence, the regulation of cell surface receptors by AnxA6 may be facilitated by its unique structure that allows recruitment of interaction partners and simultaneously bridging specialized membrane domains with cortical actin surrounding activated receptors. © 2011 IUBMB IUBMB Life, 63(11): 1009–1017, 2011