Annexins - unique membrane binding proteins with diverse functions
Annexins - unique membrane binding proteins with diverse functions
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DOI：
10.1242/jcs.01245
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发表时间：
2004-06-01
影响因子：
4
通讯作者：
Gerke, V
中科院分区：
文献类型：
--
作者：
Rescher, U;Gerke, V
膜联蛋白是钙离子调节的磷脂结合和膜结合蛋白的多基因家族。最近的工作采用膜联蛋白敲低或敲除模型提供了新的见解不同膜联蛋白的生物学功能。通过RNA干扰和显性负突变蛋白的表达的瞬时膜联蛋白耗尽揭示了从膜结构的控制到某些膜转运现象的膜过程中的蛋白质的作用。虽然这些功能与膜联蛋白以可逆和受调控的方式与细胞膜相互作用的能力密切相关，但有些活动是膜独立的，可能是因为膜联蛋白也可以参与特定的蛋白质-蛋白质相互作用。除此之外，这在膜联蛋白A1和A2敲除小鼠中是明显的，它们分别显示出中性粒细胞外渗调节受损和纤溶酶生成缺陷。
Annexins are a well-known multigene family of Ca2+-regulated phospholipid-binding and membrane-binding proteins. Recent work employing annexin-knockdown or knockout models has provided new insights into the biological functions of different annexin proteins. Transient annexin depletion by RNA interference and the expression of dominant-negative mutant proteins has revealed roles for the proteins in membrane processes ranging from the control of membrane structure to certain membrane transport phenomena. Although such functions correlate well with the ability of annexins to interact with cellular membranes in a reversible and regulated manner, some activities are membrane independent, probably because annexins can also engage in specific protein-protein interactions. Among other things, this is evident in annexin A1- and A2-knockout mice, which show impaired regulation of neutrophil extravasation and defects in plasmin generation, respectively.