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Int. J. Mol. Sci. 2013, 14(2), 2652-2683; doi:10.3390/ijms14022652
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Annexin-Phospholipid Interactions. Functional Implications

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Received: 27 December 2012; in revised form: 12 January 2013 / Accepted: 15 January 2013 / Published: 28 January 2013
(This article belongs to the Special Issue Phospholipids: Molecular Sciences 2012)
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Abstract: Annexins constitute an evolutionary conserved multigene protein superfamily characterized by their ability to interact with biological membranes in a calcium dependent manner. They are expressed by all living organisms with the exception of certain unicellular organisms. The vertebrate annexin core is composed of four (eight in annexin A6) homologous domains of around 70 amino acids, with the overall shape of a slightly bent ring surrounding a central hydrophilic pore. Calcium- and phospholipid-binding sites are located on the convex side while the N-terminus links domains I and IV on the concave side. The N-terminus region shows great variability in length and amino acid sequence and it greatly influences protein stability and specific functions of annexins. These proteins interact mainly with acidic phospholipids, such as phosphatidylserine, but differences are found regarding their affinity for lipids and calcium requirements for the interaction. Annexins are involved in a wide range of intra- and extracellular biological processes in vitro, most of them directly related with the conserved ability to bind to phospholipid bilayers: membrane trafficking, membrane-cytoskeleton anchorage, ion channel activity and regulation, as well as antiinflammatory and anticoagulant activities. However, the in vivo physiological functions of annexins are just beginning to be established.
Keywords: annexin; calcium binding; membrane aggregation; membrane binding; phospholipid binding; phosphatidylserine annexin; calcium binding; membrane aggregation; membrane binding; phospholipid binding; phosphatidylserine
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Lizarbe, M.A.; Barrasa, J.I.; Olmo, N.; Gavilanes, F.; Turnay, J. Annexin-Phospholipid Interactions. Functional Implications. Int. J. Mol. Sci. 2013, 14, 2652-2683.

AMA Style

Lizarbe MA, Barrasa JI, Olmo N, Gavilanes F, Turnay J. Annexin-Phospholipid Interactions. Functional Implications. International Journal of Molecular Sciences. 2013; 14(2):2652-2683.

Chicago/Turabian Style

Lizarbe, María A.; Barrasa, Juan I.; Olmo, Nieves; Gavilanes, Francisco; Turnay, Javier. 2013. "Annexin-Phospholipid Interactions. Functional Implications." Int. J. Mol. Sci. 14, no. 2: 2652-2683.



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