原创力文档annexin a2 at the interface of actin and membrane dynamics a focus on its roles in endocytosis and cell polarization膜联蛋白a2肌动蛋白和膜界面的动态关注它的角色在细胞内吞作用和极化.pdfVIP
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annexin a2 at the interface of actin and membrane dynamics a focus on its roles in endocytosis and cell polarization膜联蛋白a2肌动蛋白和膜界面的动态关注它的角色在细胞内吞作用和极化
Hindawi Publishing Corporation
International Journal of Cell Biology
Volume 2012, Article ID 852430, 11 pages
doi:10.1155/2012/852430
Review Article
Annexin A2 at the Interface of Actin and Membrane Dynamics:
A Focus on Its Roles in Endocytosis and Cell Polarization
Adam G. Grieve,1 Stephen E. Moss,2 and Matthew J. Hayes2
1 Hubrecht Institute for Developmental Biology and Stem Cell Research, Uppsalalaan 8, 3584CT Utrecht, The Netherlands
2 Division of Cell Biology, UCL Institute of Ophthalmology, 11-43 Bath Street, EC1V 9EL London, UK
Correspondence should be addressed to Matthew J. Hayes, annexin2@
Received 30 August 2011; Revised 16 November 2011; Accepted 13 December 2011
Academic Editor: Avri Ben-Ze’ev
Copyright © 2012 Adam G. Grieve et al. 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.
Annexins are a family of calcium- and phospholipid-binding proteins found in nearly all eukaryotes. They are structurally highly
conserved and have been implicated in a wide range of cellular activities. In this paper, we focus on Annexin A2 (AnxA2). Altered
expression of this protein has been identified in a wide variety of cancers, has also been found on the HIV particle, and has been
implicated in the maturation of the virus. Recently, it has also been shown to have an important role in the establishment of normal
apical polarity in epithelial cells. We synthesize here the known biochemical properties of this protein and the extensive literature
concerning its involvement in the endocytic pathway. We stress the importance of AnxA2 as a platform for actin remodeling in
the vicinity of dynamic cellular membr
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