Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles
Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles
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DOI：
10.1083/jcb.143.2.429
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发表时间：
1998-10-19
影响因子：
7.8
通讯作者：
Hynes, RO
中科院分区：
文献类型：
--
作者：
Borowsky, ML;Hynes, RO
细胞形态和运动性的改变由肌动蛋白细胞骨架介导。我们对微丝结构和动力学调节因子的理解的最新进展，阐明了这些改变是如何被控制的，并且人们仍在继续努力确定这些过程中涉及的所有结构和信号成分。与肌动蛋白细胞骨架相关的蛋白质踝蛋白与整合素、纽蛋白和肌动蛋白结合。我们报道了一种踝蛋白的新结合伴侣，我们将其命名为透明质酸受体（layilin），它与C型凝集素具有同源性，存在于许多细胞系和组织提取物中，并在细胞表面表达。透明质酸受体与踝蛋白在膜皱褶中共定位，并且在体外创伤实验中诱导迁移的细胞的膜皱褶以及铺展细胞的周边皱褶中被募集。透明质酸受体胞质结构域中的一个十氨基酸基序足以与踝蛋白结合。我们已经在踝蛋白的氨基末端435个氨基酸内鉴定出一个短区域，该区域能够在体外与透明质酸受体结合。这个区域与粘着斑激酶的一个结合位点重叠。
Changes in cell morphology and motility are mediated by the actin cytoskeleton. Recent advances in our understanding of the regulators of microfilament structure and dynamics have shed light on how these changes are controlled, and efforts continue to define all the structural and signaling components involved in these processes. The actin cytoskeleton-associated protein talin binds to integrins, vinculin, and actin. We report a new binding partner for talin that we have named layilin, which contains homology with C-type lectins, is present in numerous cell, lines and tissue extracts, and is expressed on the cell surface. Layilin colocalizes with talin in membrane ruffles, and is recruited to membrane ruffles in cells induced to migrate in in vitro wounding experiments and in peripheral ruffles in spreading cells. A ten-amino acid motif in the layilin cytoplasmic domain is sufficient for talin binding. We have identified a short region within talin's amino-terminal 435 amino acids capable of binding to layilin in vitro. This region overlaps a binding site for focal adhesion kinase.