ArticleBMC genomics2010
A genome-wide study of PDZ-domain interactions in C. elegans reveals a high frequency of non-canonical binding.
Article in BMC genomics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Synaptic proteomics identifies cathepsin B as a regulator of synapse remodelling during learning.bioRxiv : the preprint server for biology · 2026Article
- Analysis ofComputational and structural biotechnology journal · 2024Article
- Protein-lipid interactions drive presynaptic assembly upstream of cell adhesion molecules.bioRxiv : the preprint server for biology · 2023Article
- Review
- Transcellular chaperone signaling is an intercellular stress-response distinct from the HSF-1-mediated heat shock response.PLoS biology · 2023Article
- The unexpected versatility of ALP/Enigma family proteins.Frontiers in cell and developmental biology · 2022Review
- Viral PDZ Binding Motifs Influence Cell Behavior Through the Interaction with Cellular Proteins Containing PDZ Domains.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Article
- Intrinsic and extrinsic mechanisms of synapse formation and specificity in C. elegans.Cellular and molecular life sciences : CMLS · 2019Review
- PDZ Domains as Drug Targets.Advanced therapeutics · 2019Review
- Protein interactome mapping inCurrent opinion in systems biology · 2019Review
- Emerging Themes in PDZ Domain Signaling: Structure, Function, and Inhibition.International review of cell and molecular biology · 2019Review
- Article
- The R148.3 Gene ModulatesG3 (Bethesda, Md.) · 2017Article
- Cryptic protein-protein interaction motifs in the cytoplasmic domain of MHCI proteins.BMC immunology · 2016Article
- High-throughput methods for identification of protein-protein interactions involving short linear motifs.Cell communication and signaling : CCS · 2015Article
- Biochemical Large-Scale Interaction Analysis of Murine Olfactory Receptors and Associated Signaling Proteins with Post-Synaptic Density 95, Drosophila Discs Large, Zona-Occludens 1 (PDZ) Domains.Molecular & cellular proteomics : MCP · 2015Article
- Structures of the human Pals1 PDZ domain with and without ligand suggest gated access of Crb to the PDZ peptide-binding groove.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Characterization of diverse internal binding specificities of PDZ domains by yeast two-hybrid screening of a special peptide library.PloS one · 2014Article
- Mechanisms of NOS1AP action on NMDA receptor-nNOS signaling.Frontiers in cellular neuroscience · 2014Review
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6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundProteins may evolve through the recruitment and modification of discrete domains, and in many cases, protein action can be dissected at the domain level. PDZ domains are found in many important structural and signaling complexes, and are generally thought to interact with their protein partners through a C-terminal consensus sequence. We undertook a comprehensive search for protein partners of all individual PDZ domains in C. elegans to characterize their function and mode of interaction.
resultsCoupling high-throughput yeast two-hybrid screens with extensive validation by co-affinity purification, we defined a domain-orientated interactome map. This integrates PDZ domain proteins in numerous cell-signaling pathways and shows that PDZ domain proteins are implicated in an unexpectedly wide range of cellular processes. Importantly, we uncovered a high frequency of non-canonical interactions, not involving the C-terminus of the protein partner, which were directly confirmed in most cases. We completed our study with the generation of a yeast array representing the entire set of PDZ domains from C. elegans and provide a proof-of-principle for its application to the discovery of PDZ domain targets for any protein or peptide of interest.
conclusionsWe provide an extensive domain-centered dataset, together with a clone resource, that will help future functional study of PDZ domains. Through this unbiased approach, we revealed frequent non-canonical interactions between PDZ domains and their protein partners that will require a re-evaluation of this domain's molecular function.[The protein interactions from this publication have been submitted to the IMEx (http://www.imexconsortium.org) consortium through IntAct (PMID: 19850723) and assigned the identifier IM-14654].
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