血管扩张刺激磷蛋白（VASP）与纽蛋白的相互作用：与富含脯氨酸基序相互作用的一个反复出现的主题。

VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs.

作者信息

Reinhard M, Rüdiger M, Jockusch B M, Walter U

机构信息

Medizinische Universitätsklinik, Institut für Klinische Biochemie undPathobiochemie, Würzburg, Germany.

出版信息

FEBS Lett. 1996 Dec 9;399(1-2):103-7. doi: 10.1016/s0014-5793(96)01295-1.

DOI:10.1016/s0014-5793(96)01295-1

PMID:8980130

Abstract

VASP (vasodilator-stimulated phosphoprotein), a protein associated with microfilaments at cellular contact sites, has been identified as a ligand for profilin and zyxin, two proteins also involved in microfilament dynamics and organization at these regions. Here, we report that VASP also directly binds to vinculin, another component of adherens junctions. Competition experiments with a vinculin-derived peptide showed that a proline-rich motif, located in the hinge region that connects vinculin's head and tail domains, is involved in VASP binding. The same motif is present in zyxin but the interactions of VASP with vinculin and zyxin differ in detail. Hence, this motif may be recognized by VASP in different ways when presented in distinct cellular sites.

摘要

血管扩张刺激磷蛋白（VASP）是一种在细胞接触部位与微丝相关的蛋白质，已被鉴定为与肌动蛋白结合蛋白和斑联蛋白的配体，这两种蛋白质也参与这些区域的微丝动力学和组织。在此，我们报道VASP还直接与黏附连接的另一个成分纽蛋白结合。用纽蛋白衍生肽进行的竞争实验表明，位于连接纽蛋白头部和尾部结构域的铰链区的富含脯氨酸基序参与了VASP结合。斑联蛋白中也存在相同的基序，但VASP与纽蛋白和斑联蛋白的相互作用在细节上有所不同。因此，当该基序出现在不同的细胞位点时，可能会被VASP以不同方式识别。