Premium
Evidence for annexin A 6‐dependent plasma membrane remodelling of lipid domains
Author(s) -
AlvarezGuaita Anna,
Vilà de Muga Sandra,
Owen Dylan M,
Williamson David,
Magenau Astrid,
GarcíaMelero Ana,
Reverter Meritxell,
Hoque Monira,
Cairns Rose,
Cornely Rhea,
Tebar Francesc,
Grewal Thomas,
Gaus Katharina,
AyalaSanmartín Jesús,
Enrich Carlos,
Rentero Carles
Publication year - 2015
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/bph.13022
Subject(s) - lipid raft , microbiology and biotechnology , cytoskeleton , laurdan , actin cytoskeleton , chemistry , membrane protein , annexin a2 , actin , cell membrane , annexin , membrane , membrane fluidity , biology , cell , biochemistry , signal transduction
Annexin A6 (AnxA6) is a calcium-dependent phospholipid-binding protein that can be recruited to the plasma membrane to function as a scaffolding protein to regulate signal complex formation, endo- and exocytic pathways as well as distribution of cellular cholesterol. Here, we have investigated how AnxA6 influences the membrane order.