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Effects of the association of the αvβ8 lower legs on integrin ligand binding
Journal of Cellular Biochemistry ( IF 3.0 ) Pub Date : 2021-02-22 , DOI: 10.1002/jcb.29912 Guannan Song 1 , Bing-Hao Luo 1
Journal of Cellular Biochemistry ( IF 3.0 ) Pub Date : 2021-02-22 , DOI: 10.1002/jcb.29912 Guannan Song 1 , Bing-Hao Luo 1
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Many integrins transmit signals through global conformational changes. However, it is unclear whether integrin αvβ8 adopts a similar mechanism during integrin activation and signaling on the cell surface. Here, we showed that disulfide-bonded mutants, which prevented integrin αvβ8 lower leg dissociation, bound ligands with similar level as the wild-type protein, suggesting that αvβ8 ligand binding did not require lower leg disassociation. We further showed that the N-glycosylation mutant at the interface between the β I and hybrid domains did not affect ligand binding, suggesting that the αvβ8 open headpiece was not present on the cell surface. We proposed that αvβ8 integrin may adopt only one state, that is, the extended conformation with a closed headpiece. Our results showed that two lower legs retained heterodimeric interfaces, and this association might be important for stabilizing integrin in the extended conformation. Therefore, αvβ8 may not transmit bidirectional signals across the plasma membrane but instead may serve as an anchoring site with high affinity and high accessibility for extracellular ligands.
中文翻译：
αvβ8小腿结合对整联蛋白配体结合的影响
许多整合素通过整体构象变化传递信号。然而，尚不清楚整合素α v β 8在整合素激活和细胞表面信号传导过程中是否采用类似的机制。在这里，我们展示了阻止整合素 α v β 8小腿解离的二硫键突变体，结合配体的水平与野生型蛋白质相似，表明 α v β 8配体结合不需要小腿解离。我们进一步表明，β I 和杂交域之间界面处的 N-糖基化突变体不影响配体结合，表明 α v β 8细胞表面上不存在开放式头盔。我们提出α v β 8整联蛋白可能只采用一种状态，即具有封闭头饰的扩展构象。我们的结果表明两条小腿保留了异二聚体界面，这种关联对于稳定扩展构象中的整合素可能很重要。因此，α v β 8可能不会跨质膜传输双向信号，而是可以作为对细胞外配体具有高亲和力和高可及性的锚定位点。
更新日期：2021-02-22
中文翻译：
αvβ8小腿结合对整联蛋白配体结合的影响
许多整合素通过整体构象变化传递信号。然而，尚不清楚整合素α v β 8在整合素激活和细胞表面信号传导过程中是否采用类似的机制。在这里，我们展示了阻止整合素 α v β 8小腿解离的二硫键突变体，结合配体的水平与野生型蛋白质相似，表明 α v β 8配体结合不需要小腿解离。我们进一步表明，β I 和杂交域之间界面处的 N-糖基化突变体不影响配体结合，表明 α v β 8细胞表面上不存在开放式头盔。我们提出α v β 8整联蛋白可能只采用一种状态，即具有封闭头饰的扩展构象。我们的结果表明两条小腿保留了异二聚体界面，这种关联对于稳定扩展构象中的整合素可能很重要。因此，α v β 8可能不会跨质膜传输双向信号，而是可以作为对细胞外配体具有高亲和力和高可及性的锚定位点。
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