Annexin A2 Heterotetramer: Structure and Function
نویسندگان
چکیده
Annexin A2 is a pleiotropic calcium- and anionic phospholipid-binding protein that exists as a monomer and as a heterotetrameric complex with the plasminogen receptor protein, S100A10. Annexin A2 has been proposed to play a key role in many processes including exocytosis, endocytosis, membrane organization, ion channel conductance, and also to link F-actin cytoskeleton to the plasma membrane. Despite an impressive list of potential binding partners and regulatory activities, it was somewhat unexpected that the annexin A2-null mouse should show a relatively benign phenotype. Studies with the annexin A2-null mouse have suggested important functions for annexin A2 and the heterotetramer in fibrinolysis, in the regulation of the LDL receptor and in cellular redox regulation. However, the demonstration that depletion of annexin A2 causes the depletion of several other proteins including S100A10, fascin and affects the expression of at least sixty-one genes has confounded the reports of its function. In this review we will discuss the annexin A2 structure and function and its proposed physiological and pathological roles.
منابع مشابه
Identification of the annexin A2 heterotetramer as a receptor for the plasmin-induced signaling in human peripheral monocytes.
We have previously demonstrated that plasmin acts as a potent proinflammatory activator of human peripheral monocytes. Here we identify the annexin A2 heterotetramer, composed of annexin A2 and S100A10, as a receptor for the plasmin-induced signaling in human monocytes. Monocytes express the annexin A2 heterotetramer on the cell surface as shown by flow cytometry, fluorescence microscopy, and c...
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BACKGROUND Annexin A2 is a peripheral membrane protein that belongs to the annexin family of Ca(2+) and phospholipid-binding proteins. This protein, which plays a role in membrane organization and dynamics in particular along the endocytic pathway, exists as a heterotetrameric complex, consisting of two annexin A2 molecules bound via their N-termini to a dimer of p11/S100A10 light chains. The l...
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عنوان ژورنال:
دوره 14 شماره
صفحات -
تاریخ انتشار 2013