The actin-bundling protein L-plastin: a critical regulator of immune cell function.
The actin-bundling protein L-plastin: a critical regulator of immune cell function.
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DOI：
10.1155/2012/935173
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发表时间：
2012
影响因子：
--
通讯作者：
Morley SC
中科院分区：
文献类型：
--
作者：
Morley SC
L-纤溶酶原是一种白细胞特异性蛋白质，可将肌动蛋白丝交联成紧密的纤维束，增加肌动蛋白基结构（如podosomes和lamellipodia）的稳定性。虽然在25年前首次被鉴定为造血衍生细胞中丰富的细胞质蛋白，但在免疫关键的多个功能（如抗原受体信号传导、粘附和运动性）中对L-塑性蛋白的需求最近才变得清楚。L-纤维蛋白原已被确定为对中性粒细胞、巨噬细胞、破骨细胞、嗜酸性粒细胞以及T-和B-淋巴细胞生物学至关重要的细胞过程中的重要组分。在简要介绍L-plastin的结构和功能后，将详细综述L-plastin对免疫细胞功能的调节。
L-plastin is a leukocyte-specific protein that cross-links actin filaments into tight bundles, increasing the stability of actin-based structures such as podosomes and lamellipodia. While first identified as an abundant cytoplasmic protein in hematopoietically derived cells over 25 years ago, the requirement for L-plastin in multiple functions critical for immunity, such as antigen receptor signaling, adhesion, and motility, has only recently become clear. L-plastin has been identified as an important component in cellular processes critical for neutrophil, macrophage, osteoclast, eosinophil, and T- and B-lymphocyte biology. Following a brief description of the structure and function of L-plastin, the regulation of immune cell functions by L-plastin will be reviewed in detail.