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  • 标题:Binding of the protein ICln to α-integrin contributes to the activation of IClswell current
  • 本地全文:下载
  • 作者:Andreas Schedlbauer ; Grazia Tamma ; Simona Rodighiero
  • 期刊名称:Scientific Reports
  • 电子版ISSN:2045-2322
  • 出版年度:2019
  • 卷号:9
  • 期号:1
  • 页码:1-16
  • DOI:10.1038/s41598-019-48496-4
  • 出版社:Springer Nature
  • 摘要:ICl swell is the chloride current induced by cell swelling, and plays a fundamental role in several biological processes, including the regulatory volume decrease (RVD). ICln is a highly conserved, ubiquitously expressed and multifunctional protein involved in the activation of ICl swell . In platelets, ICln binds to the intracellular domain of the integrin αIIb chain, however, whether the ICln/integrin interaction plays a role in RVD is not known. Here we show that a direct molecular interaction between ICln and the integrin α-chain is not restricted to platelets and involves highly conserved amino acid motifs. Integrin α recruits ICln to the plasma membrane, thereby facilitating the activation of ICl swell during hypotonicity. Perturbation of the ICln/integrin interaction prevents the transposition of ICln towards the cell surface and, in parallel, impedes the activation of ICl swell . We suggest that the ICln/integrin interaction interface may represent a new molecular target enabling specific ICl swell suppression in pathological conditions when this current is deregulated or plays a detrimental role.
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