ArticleMolecular & cellular proteomics : MCP2008
Monitoring protein-protein interactions between the mammalian integral membrane transporters and PDZ-interacting partners using a modified split-ubiquitin membrane yeast two-hybrid system.
Article in Molecular & cellular proteomics : MCP, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 88 citations in OpenAlex.
- Structures of the sodium-coupled phosphate importer SLC34A2 reveal a distinct architecture and gating mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Integrated Membrane Yeast Two-Hybrid System for the Analysis of Membrane Protein Complexes.Bio-protocol · 2025Article
- Article
- PDZ Peptide of the ZO-1 Protein Significantly Increases UTP-InducedMolecules and cells · 2023Article
- Topology, tissue distribution, and transcriptional level of SLC34s in response to Pi and pH in grass carp Ctenopharyngodon idella.Fish physiology and biochemistry · 2021Article
- The Arg/N-degron pathway targets transcription factors and regulates specific genes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- High-Throughput Identification of Nuclear Envelope Protein Interactions inG3 (Bethesda, Md.) · 2020Article
- Sodium-coupled glucose transport, the SLC5 family, and therapeutically relevant inhibitors: from molecular discovery to clinical application.Pflugers Archiv : European journal of physiology · 2020Review
- The ATF3 Transcription Factor Is a Short-Lived Substrate of the Arg/N-Degron Pathway.Biochemistry · 2020Article
- Mechanisms of phosphate transport.Nature reviews. Nephrology · 2019Review
- Review
- Renal phosphate handling and inherited disorders of phosphate reabsorption: an update.Pediatric nephrology (Berlin, Germany) · 2019Review
- NaPi-IIa interacting partners and their (un)known functional roles.Pflugers Archiv : European journal of physiology · 2019Review
- The Methods Employed in Mass Spectrometric Analysis of Posttranslational Modifications (PTMs) and Protein-Protein Interactions (PPIs).Advances in experimental medicine and biology · 2019Review
- Clinical aspects of the phosphate transporters NaPi-IIa and NaPi-IIb: mutations and disease associations.Pflugers Archiv : European journal of physiology · 2019Review
- The molecular mechanism of SLC34 proteins: insights from two decades of transport assays and structure-function studies.Pflugers Archiv : European journal of physiology · 2019Review
- Molecular Studies of the Protein Complexes InvolvingFrontiers in plant science · 2019Article
- Dopamine reduces cell surface NaAmerican journal of physiology. Renal physiology · 2017Article
- Systematic protein-protein interaction mapping for clinically relevant human GPCRs.Molecular systems biology · 2017Article
- MAP17 Is a Necessary Activator of Renal Na+/Glucose Cotransporter SGLT2.Journal of the American Society of Nephrology : JASN · 2017Article
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12 authors at 5 institutions in 4 countries.
Funding
Abstract
PDZ-binding motifs are found in the C-terminal tails of numerous integral membrane proteins where they mediate specific protein-protein interactions by binding to PDZ-containing proteins. Conventional yeast two-hybrid screens have been used to probe protein-protein interactions of these soluble C termini. However, to date no in vivo technology has been available to study interactions between the full-length integral membrane proteins and their cognate PDZ-interacting partners. We previously developed a split-ubiquitin membrane yeast two-hybrid (MYTH) system to test interactions between such integral membrane proteins by using a transcriptional output based on cleavage of a transcription factor from the C terminus of membrane-inserted baits. Here we modified MYTH to permit detection of C-terminal PDZ domain interactions by redirecting the transcription factor moiety from the C to the N terminus of a given integral membrane protein thus liberating their native C termini. We successfully applied this "MYTH 2.0" system to five different mammalian full-length renal transporters and identified novel PDZ domain-containing partners of the phosphate (NaPi-IIa) and sulfate (NaS1) transporters that would have otherwise not been detectable. Furthermore this assay was applied to locate the PDZ-binding domain on the NaS1 protein. We showed that the PDZ-binding domain for PDZK1 on NaS1 is upstream of its C terminus, whereas the two interacting proteins, NHERF-1 and NHERF-2, bind at a location closer to the N terminus of NaS1. Moreover NHERF-1 and NHERF-2 increased functional sulfate uptake in Xenopus oocytes when co-expressed with NaS1. Finally we used MYTH 2.0 to demonstrate that the NaPi-IIa transporter homodimerizes via protein-protein interactions within the lipid bilayer. In summary, our study establishes the MYTH 2.0 system as a novel tool for interactive proteomics studies of membrane protein complexes.
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