Binding of the protein ICln to α-integrin contributes to the activation of IClswell current.

Scientific reports 2019 Aug 21

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IClswell 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 IClswell. 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 IClswell during hypotonicity. Perturbation of the ICln/integrin interaction prevents the transposition of ICln towards the cell surface and, in parallel, impedes the activation of IClswell. We suggest that the ICln/integrin interaction interface may represent a new molecular target enabling specific IClswell suppression in pathological conditions when this current is deregulated or plays a detrimental role.

Citation

Andreas Schedlbauer, Grazia Tamma, Simona Rodighiero, Davide Antonio Civello, Margherita Tamplenizza, Karin Ledolter, Charity Nofziger, Wolfgang Patsch, Robert Konrat, Markus Paulmichl, Silvia Dossena. Binding of the protein ICln to α-integrin contributes to the activation of IClswell current. Scientific reports. 2019 Aug 21;9(1):12195