Paxillin: a new vinculin-binding protein present in focal adhesions.
Paxillin: a new vinculin-binding protein present in focal adhesions.
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DOI：
10.1083/jcb.111.3.1059
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发表时间：
1990-09
影响因子：
7.8
通讯作者：
Burridge, K
中科院分区：
文献类型：
--
作者：
Turner, C E;Glenney, J R Jr;Burridge, K
68-kD蛋白（paxillin）是一种细胞骨架成分，定位于鸡胚成纤维细胞肌动蛋白应激纤维末端的局灶粘连。它也存在于马丁-达比牛肾（MDBK）上皮细胞的局灶黏附中，但像talin一样，不存在于这些细胞的细胞-细胞黏附连接中。从鸡胗平滑肌中纯化的Paxillin在SDS- PAGE凝胶上呈弥漫性条带迁移，分子量为65- 70kd。它是一种具有多种同工异构体的蛋白质，pi在6.31到6.85之间。使用纯化的paxillin，我们已经证明了与另一种黏附蛋白，vinculin的体外特异性相互作用。与金黄色葡萄球菌V8蛋白酶的切割导致产生两个约85和27 kD的片段。与talin不同，它与大的血管蛋白片段结合，paxillin被发现与小的血管蛋白片段结合，这代表了分子的棒状结构域。与先前观察到的paxillin是劳斯肉瘤病毒转化细胞中pp60src的主要底物（Glenney， J. R. and L. Zokas. 1989）。J.细胞生物学。108:2401-2408)，这种与vinculin的相互作用表明paxillin可能是控制局点粘附组织的关键成分。
The 68-kD protein (paxillin) is a cytoskeletal component that localizes to the focal adhesions at the ends of actin stress fibers in chicken embryo fibroblasts. It is also present in the focal adhesions of Madin- Darby bovine kidney (MDBK) epithelial cells but is absent, like talin, from the cell-cell adherens junctions of these cells. Paxillin purified from chicken gizzard smooth muscle migrates as a diffuse band on SDS- PAGE gels with a molecular mass of 65-70 kD. It is a protein of multiple isoforms with pIs ranging from 6.31 to 6.85. Using purified paxillin, we have demonstrated a specific interaction in vitro with another focal adhesion protein, vinculin. Cleavage of vinculin with Staphylococcus aureus V8 protease results in the generation of two fragments of approximately 85 and 27 kD. Unlike talin, which binds to the large vinculin fragment, paxillin was found to bind to the small vinculin fragment, which represents the rod domain of the molecule. Together with the previous observation that paxillin is a major substrate of pp60src in Rous sarcoma virus-transformed cells (Glenney, J. R., and L. Zokas. 1989. J. Cell Biol. 108:2401-2408), this interaction with vinculin suggests paxillin may be a key component in the control of focal adhesion organization.