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ICl 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. 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 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. We suggest that the ICln/integrin interaction interface may represent a new molecular target enabling specific ICl suppression in pathological conditions when this current is deregulated or plays a detrimental role.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6704128 | PMC |
| http://dx.doi.org/10.1038/s41598-019-48496-4 | DOI Listing |
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