ArticleNature communications2024
ReLo is a simple and rapid colocalization assay to identify and characterize direct protein-protein interactions.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- A co-overexpression strategy allows effective protein-protein binding affinities to be assessed as a function of concentration within live cells.bioRxiv : the preprint server for biology · 2026Article
- Conserved RNA helicase Vasa regulates ribonucleoprotein condensate dynamics and mRNA localization.iScience · 2026Article
- Nek1 defines a branch of centriolar microtubule length control parallel to CP110-Cep97.Nature communications · 2026Article
- Disrupting the ASH2L-DPY30 PPI in cancer: structure, function, and therapeutic opportunities in H3K4 methylation.Epigenetics & chromatin · 2026Review
- Recurrent innovation of protein-protein interactions in the Drosophila piRNA pathway.The EMBO journal · 2026Article
- Conserved RNA helicase Vasa regulates ribonucleoprotein condensates through protein interaction and mRNA recruitment.bioRxiv : the preprint server for biology · 2025Article
- Towards a phylogenetically informed approach to solving protein-protein interactions.Biochemical Society transactions · 2025Review
- Probing direct interactions between nuclear proteins in cells with nxReLo.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular insights into the Drosophila piRNA pathway via systematic ReLo protein interaction screening and structure prediction.Nucleic acids research · 2025Article
- Multivalent interactions with CCR4-NOT and PABPC1 determine mRNA repression efficiency by tristetraprolin.Nature communications · 2025Article
- Imaging the Binding Between Dasatinib and Its Target Protein in Living Cells Using an SLP Tag System on Intracellular Compartments.International journal of molecular sciences · 2025Article
- Redox Enzymes P4HB and PDIA3 Interact with STIM1 to Fine-Tune Its Calcium Sensitivity and Activation.International journal of molecular sciences · 2024Article
- Structural basis for binding ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system.Nucleic acids research · 2023Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The characterization of protein-protein interactions (PPIs) is fundamental to the understanding of biochemical processes. Many methods have been established to identify and study direct PPIs; however, screening and investigating PPIs involving large or poorly soluble proteins remains challenging. Here, we introduce ReLo, a simple, rapid, and versatile cell culture-based method for detecting and investigating interactions in a cellular context. Our experiments demonstrate that ReLo specifically detects direct binary PPIs. Furthermore, we show that ReLo bridging experiments can also be used to determine the binding topology of subunits within multiprotein complexes. In addition, ReLo facilitates the identification of protein domains that mediate complex formation, allows screening for interfering point mutations, and it is sensitive to drugs that mediate or disrupt an interaction. In summary, ReLo is a simple and rapid alternative for the study of PPIs, especially when studying structurally complex proteins or when established methods fail.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.