STRUCTURE OF INTEGRIN, A GLYCOPROTEIN INVOLVED IN THE TRANSMEMBRANE LINKAGE BETWEEN FIBRONECTIN AND ACTIN
STRUCTURE OF INTEGRIN, A GLYCOPROTEIN INVOLVED IN THE TRANSMEMBRANE LINKAGE BETWEEN FIBRONECTIN AND ACTIN
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DOI：
10.1016/0092-8674(86)90744-0
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发表时间：
1986-07-18
期刊：
影响因子：
64.5
通讯作者：
HYNES, RO
中科院分区：
文献类型：
--
作者：
TAMKUN, JW;DESIMONE, DW;HYNES, RO
我们描述了编码膜糖蛋白复合体的一个亚基的cDNA克隆的分离、鉴定和测序，该复合体构成了细胞外基质和细胞骨架之间跨膜连接的一部分。该序列编码一个89kd的多肽，其特征强烈表明存在一个大的N-末端胞外结构域、一个单一的跨膜片段和一个小的C-末端胞质结构域。胞外区包含一个新的富含半胱氨酸的40个残基的三倍重复片段，胞内区包含一个酪氨酸残基，该残基是酪氨酸激酶的潜在磷酸化位点。我们建议将这个蛋白质复合体命名为整合素，以表示它作为一个完整的膜复合体参与细胞外基质和细胞骨架之间的跨膜结合。
We describe the isolation, characterization, and sequence of cDNA clones encoding one subunit of the complex of membrane glycoproteins that forms part of the transmembrane connection between the extracellular matrix and the cytoskeleton. The cDNA sequence encodes a polypeptide of 89 kd that has features strongly suggesting the presence of a large N-terminal extracellular domain, a single transmembrane segment, and a small C-terminal cytoplasmic domain. The extracellular domain contains a threefold repeat of a novel 40 residue cysteine-rich segment, and the cytoplasmic domain contains a tyrosine residue that is a potential site for phosphorylation by tyrosine kinases. We propose the name integrin for this protein complex to denote its role as an integral membrane complex involved in the transmembrane association between the extracellular matrix and the cytoskeleton.