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- W2044268514 endingPage "6305" @default.
- W2044268514 startingPage "6259" @default.
- W2044268514 abstract "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." @default.
- W2044268514 created "2016-06-24" @default.
- W2044268514 creator A5012449534 @default.
- W2044268514 creator A5072439778 @default.
- W2044268514 creator A5091852858 @default.
- W2044268514 creator A5011227157 @default.
- W2044268514 date "2013-03-19" @default.
- W2044268514 modified "2023-10-16" @default.
- W2044268514 title "Annexin A2 Heterotetramer: Structure and Function" @default.
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