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

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... Mehr ...

Verfasser: Ben C. Tilly
Martin Jakab
Markus Ritter
Robert Konrat
Rosaria Gandini
Johannes Fürst
Claudia Bazzini
Giuliano Meyer
Markus Paulmichl
S. Saino
Maria Lisa Garavaglia
Andreas Schedlbauer
Martin Gschwentner
Guido Bottà
Bettina Sarg
Georg Kontaxis
Herbert Lindner
Dokumenttyp: Artikel
Erscheinungsdatum: 2005
Schlagwörter: Netherlands / Cell Biology / Molecular Biology / Biochemistry
Sprache: Englisch
Permalink: https://search.fid-benelux.de/Record/base-26811810
Datenquelle: BASE; Originalkatalog
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Link(s) : https://www.openaccessrepository.it/record/95469