ArticleStructure (London, England : 1993)2011
Structural basis for complex formation between human IRSp53 and the translocated intimin receptor Tir of enterohemorrhagic E. coli.
Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- Why put yourself on a pedestal? The pathogenic role of the A/E pedestal.Infection and immunity · 2024Review
- The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection.Communications biology · 2024Article
- Using Linear Motif Database Resources to Identify SH2 Domain Binders.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Short linear motif candidates in the cell entry system used by SARS-CoV-2 and their potential therapeutic implications.Science signaling · 2021Review
- Lipid-Composition-Mediated Forces Can Stabilize Tubular Assemblies of I-BAR Proteins.Biophysical journal · 2021Article
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- ELM-the eukaryotic linear motif resource in 2020.Nucleic acids research · 2020Article
- Unusual Organization of I-BAR Proteins on Tubular and Vesicular Membranes.Biophysical journal · 2019Article
- EnterohemorrhagicEmerging microbes & infections · 2019Article
- IRTKS (BAIAP2L1) Elongates Epithelial Microvilli Using EPS8-Dependent and Independent Mechanisms.Current biology : CB · 2018Article
- BAI1-Associated Protein 2-Like 1 (BAIAP2L1) Is a Potential Biomarker in Ovarian Cancer.PloS one · 2015Article
- Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors.Nature structural & molecular biology · 2014Article
- Intimate host attachment: enteropathogenic and enterohaemorrhagic Escherichia coli.Cellular microbiology · 2013Review
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- Bacterial scaffolds assemble novel higher-order complexes to reengineer eukaryotic cell processes.Science signaling · 2011Article
- EHEC Adhesins.Microbiology spectrumArticle
Corrections and comments
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Authors and funding
14 authors at 6 institutions in 2 countries.
Funding
Abstract
Actin assembly beneath enterohemorrhagic E. coli (EHEC) attached to its host cell is triggered by the intracellular interaction of its translocated effector proteins Tir and EspF(U) with human IRSp53 family proteins and N-WASP. Here, we report the structure of the N-terminal I-BAR domain of IRSp53 in complex with a Tir-derived peptide, in which the homodimeric I-BAR domain binds two Tir molecules aligned in parallel. This arrangement provides a protein scaffold linking the bacterium to the host cell's actin polymerization machinery. The structure uncovers a specific peptide-binding site on the I-BAR surface, conserved between IRSp53 and IRTKS. The Tir Asn-Pro-Tyr (NPY) motif, essential for pedestal formation, is specifically recognized by this binding site. The site was confirmed by mutagenesis and in vivo-binding assays. It is possible that IRSp53 utilizes the NPY-binding site for additional interactions with as yet unknown partners within the host cell.
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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 OpenQuestion graph.