纤维连接蛋白/整合素相互作用诱导120 kda蛋白的酪氨酸磷酸化。

J L Guan, J E Trevithick, R O Hynes
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引用次数: 503

摘要

我们描述了一种120 kda的蛋白(pp120),它在附着于纤维连接蛋白涂层表面的细胞中被酪氨酸磷酸化。该蛋白似乎位于与β 1整合素共分布的病灶接触处。Pp120不同于整合素的β 1亚基,也不同于血管蛋白和α -肌动蛋白。Pp120在胰蛋白酶化悬浮的细胞中迅速去磷酸化,但在附着和扩散在纤维连接蛋白上的细胞中迅速磷酸化。细胞附着在含有rgd的肽、聚赖氨酸或豆豆蛋白A上并不足以诱导pp120的磷酸化。纤连蛋白的120-kDa细胞结合域可以诱导pp120的部分磷酸化,但进一步的磷酸化也会在纤连蛋白的肝素结合域存在的情况下发生。pp120的磷酸化先于细胞扩散,但与随后的细胞扩散相关。pp120的磷酸化也可以通过细胞附着到抗整合素抗体上触发,这需要整合素- 1亚基的细胞质结构域。因此β 1整合素与细胞外配体(纤维连接蛋白或抗体)的相互作用触发细胞内120-kDa蛋白pp120的磷酸化,这可能参与细胞对附着的反应。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein.

We describe a 120-kDa protein (pp120) that is phosphorylated on tyrosine in cells attached to fibronectin-coated surfaces. The protein appears to be located in focal contacts where it codistributes with beta 1 integrins. pp120 is distinct from the beta 1 subunit of integrins and from vinculin and alpha-actinin. pp120 is rapidly dephosphorylated in cells suspended by trypsinization but becomes rapidly phosphorylated in cells attaching and spreading on fibronectin. Attachment of cells to RGD-containing peptides, polylysine, or concanavalin A is not sufficient to induce phosphorylation of pp120. The 120-kDa cell-binding domain of fibronectin can induce some phosphorylation of pp120, but further phosphorylation occurs in the presence also of the heparin-binding domain of fibronectin. Phosphorylation of pp120 precedes, but is correlated with, subsequent cell spreading. Phosphorylation of pp120 can also be triggered by attachment of cells to anti-integrin antibodies, and this requires the cytoplasmic domain of the integrin beta 1 subunit. Thus interaction of beta 1 integrins with extracellular ligands (fibronectin or antibodies) triggers phosphorylation of an intracellular 120-kDa protein, pp120, that may be involved in the responses of cells to attachment.

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