AN ACTIN-BINDING SITE CONTAINING A CONSERVED MOTIF OF CHARGED AMINO-ACID-RESIDUES IS ESSENTIAL FOR THE MORPHOGENIC EFFECT OF VILLIN
AN ACTIN-BINDING SITE CONTAINING A CONSERVED MOTIF OF CHARGED AMINO-ACID-RESIDUES IS ESSENTIAL FOR THE MORPHOGENIC EFFECT OF VILLIN
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DOI：
10.1016/0092-8674(92)90535-k
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发表时间：
1992-07-10
期刊：
影响因子：
64.5
通讯作者：
LOUVARD, D
中科院分区：
文献类型：
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作者：
FRIEDERICH, E;VANCOMPERNOLLE, K;LOUVARD, D
肌动蛋白结合蛋白在正常情况下不产生该蛋白的细胞中诱导微绒毛生长和细胞骨架的重组。将诱变的绒毛蛋白cDNA导入CV-1细胞，结果表明，一个保守的、位于COOH末端的带电氨基酸残基簇(KKEK)在体内对绒毛蛋白的形态发生活性起着至关重要的作用。体外实验表明，这个基序是F-肌动蛋白结合部位的一部分，可以诱导G-肌动蛋白聚合。肌动蛋白与该多肽的化学交联、多肽中氨基酸取代的影响以及维林变异体的行为进一步证实了KKEK序列参与了肌动蛋白的接触。
The actin-binding protein villin induces microvillus growth and reorganization of the cytoskeleton in cells that do not normally produce this protein. Transfection of mutagenized villin cDNAs into CV-1 cells was used to show that a conserved, COOH-terminally located cluster of charged amino acid residues (KKEK) is crucial for the morphogenic activity of villin in vivo. In vitro experiments with a 22 amino acid synthetic peptide corresponding to this region of villin provide evidence that this motif is part of an F-actin-binding site that induces G-actin to polymerize. Chemical cross-linking of actin to this peptide, the effects of amino acid substitutions in peptides, and the behavior of villin variants further corroborate the participation of the KKEK sequence in actin contacts.