Unraveling aquaporin interaction partners |
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Authors: | Jennie Sjöhamn Kristina Hedfalk |
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Institution: | Department of Chemistry and Molecular Biology, University of Gothenburg, P.O. Box 462, SE-405 30 Göteborg, Sweden |
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Abstract: | BackgroundInsight into protein–protein interactions (PPIs) is highly desirable in order to understand the physiology of cellular events. This understanding is one of the challenges in biochemistry and molecular biology today, especially for eukaryotic membrane proteins where hurdles of production, purification and structural determination must be passed.Scope of reviewWe have explored the common strategies used to find medically relevant interaction partners of aquaporins (AQPs). The most frequently used methods to detect direct contact, yeast two-hybrid interaction assay and co-precipitation, are described together with interactions specifically found for the selected targets AQP0, AQP2, AQP4 and AQP5.Major conclusionsThe vast majority of interactions involve the aquaporin C-terminus and the characteristics of the interaction partners are strikingly diverse. While the well-established methods for PPIs are robust, a novel approach like bimolecular fluorescence complementation (BiFC) is attractive for screening many conditions as well as transient interactions. The ultimate goal is structural evaluation of protein complexes in order to get mechanistic insight into how proteins communicate at a molecular level.General significanceWhat we learn from the human aquaporin field in terms of method development and communication between proteins can be of major use for any integral membrane protein of eukaryotic origin. This article is part of a Special Issue entitled Aquaporins. |
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Keywords: | AQP aquaporin GFP green fluorescent protein ICC immunocytochemistry IHC immunohistochemistry IP immunoprecipitation PPI protein&ndash protein interaction YTH yeast two-hybrid |
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