期刊
IUBMB LIFE
卷 63, 期 11, 页码 1009-1017出版社
WILEY
DOI: 10.1002/iub.540
关键词
annexin A6; membrane domains; actin cytoskeleton; cholesterol; calcium mediated signaling; T cell activation; epidermal growth factor
资金
- National Health and Medical Research Council of Australia (NHMRC) [510293, 510294]
- University of Sydney [2010-02681]
- Ministerio de Innovacion, Ciencia y Tecnologia [CSD2009-00016, FU2009-10335]
- Fundacio Marato TV3 (Barcelona, Spain) [PI040236]
- Beatriu de Pinos Fellowship (Generalitat de Catalunya)
- National Health and Medical Research Council of Australia
- Australian Research Council
- Human Frontier Science Program
Annexin A6 (AnxA6) belongs to the conserved annexin protein family-a group of Ca2+-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 Ca2+-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, Ca2+-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. (C) 2011 IUBMB IUBMB Life, 63(11): 1009-1017, 2011
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