ICln159 folds into a pleckstrin homology domain-like structure: Interaction with kinases and the splicing factor LSm4

Johannes Fürst, Andreas Schedlbauer, Rosaria Gandini, Maria Lisa Garavaglia, Stefano Saino, Martin Gschwentner, Bettina Sarg, Herbert Lindner, Martin Jakab, Markus Ritter, Claudia Bazzini, Guido Botta, Gabriele Meyer, Georg Kontaxis, Ben C. Tilly, Robert Konrat, Michael Paul

    Veröffentlichungen: Beitrag in FachzeitschriftArtikelPeer Reviewed


    ICln is a multifunctional protein involved in regulatory mechanisms as different as membrane ion transport and RNA splicing. The protein is water-soluble, and during regulatory volume decrease after cell swelling, it is able to migrate from the cytosol to the cell membrane. Purified, water-soluble ICln is able to insert into lipid bilayers to form ion channels. Here, we show that ICln159, a truncated ICln mutant, which is also able to form ion channels in lipid bilayers, belongs to the pleckstrin homology (PH) domain superfold family of proteins. The ICln PH domain shows unusual properties as it lacks the electrostatic surface polarization seen in classical PH domains. However, similar to many classical PH domain-containing proteins, ICln interacts with protein kinase C, and in addition, interacts with cAMP-dependent protein kinase and cGMP-dependent protein kinase type II but not cGMDP-dependent protein kinase type Iß. A major phosphorylation site for all three kinases is Ser-45 within the ICln PH domain. Furthermore, ICln159 interacts with LSm4, a protein involved in splicing and mRNA degradation, suggesting that the ICln159 PH domain may serve as a protein-protein interaction platform. Œ 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
    Seiten (von - bis)31276-31282
    FachzeitschriftJournal of Biological Chemistry
    PublikationsstatusVeröffentlicht - 2005

    ÖFOS 2012

    • 104021 Strukturchemie