Annexin II

Annexin II (other names: Annexin II, Annexin A2, Annexin 2, Lipocortin II, Calpactin I heavy chain, Chromobindin-8, p36, Placental anticoagulant protein IV).

UniProtKB/Swiss-Prot entry: P07355

The annexine 2 (Anx2) is a Protéine of 38 kDa which belongs to the family of the annexines. The annexines are proteins which have a double cytosolic cellular localization and membrane. They establish the link between calcic indication and membrane dynamics, two functions implying the same basic mechanism; their connection reversible and dependant on Ca2+. Moreover their interaction with the lipids the membrane with consequences disturbs on cellular indication.

Anx2 is structured in 2 fields: the heart which contains the sites of connection in Ca2+ persons in charge of the connection to the membranes, and the N-terminal field which has the site of connection to protein S100A10 with which it form a tetramer. The N-terminal field controls the properties of the heart by dimerisation, connection with the S100A10 and phosphorylation. In the presence of Ca2+, Anx2 binds to the plasmic membranes via anion Phospholipides such as the Phosphatidylsérine (PS) and the Phosphatidylinositol (pi) and causes also the aggregation of these membranes.

Anx2 is implied in the phenomena of Exocytose and Endocytose, coagulation, interactions membrane - Cytosquelette (Actine) and of formation of the intercellular Jonctions. In all these physiological phenomena, it interacts with several partners the main thing of them, as underlined higher, is the S100A10 called also P11. S100A10 is a protein of 11 kDa which belongs to the family of the S100 proteins. She interacts with Anx2 with a very high affinity and independently of calcium. She forms a homodimère (P11) 2 which little to fix two molecules of Anx2 to form a hétérotétramère (Anx2) 2 (P11) 2.

Anx2 in monomeric or heterotetrameric form in complex with S100A10, can bind other molecules such as the Actine to control the dynamics of the Cytosquelette and to stabilize the membrane microdomains rich in cholesterol. It also binds to Caveoline 1 to control the transport of cholesterol, with protein AHNAK to control the interactions Cytosquelette - membranes.

References

  • Gerke, V., Creutz, E.C. and Moss, S.E. (2005) Annexins: linking Ca2+ signalling to membrane dynamics. Nat.Rev.Mol.Cell Biol., 6,449-461.
  • Gerke, V. and Moss, S.E. (1997) Annexins and membrane dynamics. Biochim.Biophys.Acta, 1357,129-154.
  • Gerke, V. and Moss, S.E. (2002) Annexins: from structure to function. Physiol rev., 82,331-371.
  • Gerke, V. (2001) Annexins And Membrane Organization In The Endocytic Pathway. Mol.Biol.Lett concealment., 6,204.
  • Menke, Mr., Gerke, V. and Steinem, C. (2005) Phosphatidylserine Membrane Domain Clustering Induced by Annexin A2/S100A10 Heterotetramer. Biochemistry, 44,15296-15303.
  • Beam, M.J., Rescher, U., Gerke, V. and Moss, S.E. (2004) Annexin-actin interactions. Traffic., 5,571-576.
  • Beam, M.J., Shao, D., Bailly, Mr. and Moss, S.E. (2006) Regulation off actin dynamics by annexin 2. EMBO J., 25,1816-1826.

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