Annexins: from structure to function

Physiological Reviews
Volker Gerke, Stephen E Moss

Abstract

Annexins are Ca2+ and phospholipid binding proteins forming an evolutionary conserved multigene family with members of the family being expressed throughout animal and plant kingdoms. Structurally, annexins are characterized by a highly alpha-helical and tightly packed protein core domain considered to represent a Ca2+-regulated membrane binding module. Many of the annexin cores have been crystallized, and their molecular structures reveal interesting features that include the architecture of the annexin-type Ca2+ binding sites and a central hydrophilic pore proposed to function as a Ca2+ channel. In addition to the conserved core, all annexins contain a second principal domain. This domain, which NH2-terminally precedes the core, is unique for a given member of the family and most likely specifies individual annexin properties in vivo. Cellular and animal knock-out models as well as dominant-negative mutants have recently been established for a number of annexins, and the effects of such manipulations are strikingly different for different members of the family. At least for some annexins, it appears that they participate in the regulation of membrane organization and membrane traffic and the regulation of ion (Ca2+) currents ...Continue Reading

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Citations

Apr 20, 2014·PloS One·Yoana Arroyo-BerdugoMaría Dolores Boyano
May 17, 2014·World Journal of Gastroenterology : WJG·Hai-Lin HuangKai-Zhou Jin
Jun 6, 2014·BioMed Research International·Sajal GuptaAshok Agarwal
Jul 15, 2003·Proceedings of the National Academy of Sciences of the United States of America·Unkyu KimRobert G Roeder
Feb 27, 2004·Proceedings of the National Academy of Sciences of the United States of America·Eric J SmartSteven A Farber
Apr 3, 2004·Genome Biology·Stephen E Moss, Reg O Morgan
Apr 6, 2004·Molecular Biology of the Cell·Xiaoxuan FanRobert A Schlegel
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Jan 7, 2005·Molecular Biology of the Cell·Sylvette Chasserot-GolazMarie-France Bader
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Feb 6, 2009·The Journal of Biological Chemistry·Matthew J Hayes, Stephen E Moss
Apr 24, 2009·The Journal of Biological Chemistry·Katia MonastyrskayaAnnette Draeger

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