ArticleMolecular cell2015
A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases.
Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 57 citations in OpenAlex.
- E3 Ubiquitin Ligase Mind Bomb 1 is a Novel Negative Regulator of Tumor-Suppressive BMP Signaling.Cancer research communications · 2026Article
- Engineering synthetic agonists for targeted activation of Notch signaling.Nature chemical biology · 2026Article
- A novel peptide MIB1-223aa encoded by exosomal circMIB1 from cancer-associated fibroblasts drives triple-negative breast cancer metastasis and stemness via stabilizing MIB1 to activate Notch signaling.Journal of advanced research · 2026Article
- Neuralized-like proteins differentially activate Notch ligands.EMBO reports · 2025Article
- The intracellular domains of the DSL ligands Serrate and Delta provide different activities.Cell communication and signaling : CCS · 2025Article
- Structural basis for the recognition and ubiquitylation of type-2 N-degron substrate by PRT1 plant N-recognin.Nature communications · 2025Article
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- Hepatocyte-Targeted Lipid Nanoparticle Delivery of HERC2 Plasmid Controls Drug-Induced Hepatotoxicity by Limiting β-Catenin-Regulated CYP2E1 Expression.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Structural requirements for activity of Mind bomb1 in Notch signaling.Structure (London, England : 1993) · 2024Article
- Temporal dynamics and stoichiometry in human Notch signaling from Notch synaptic complex formation to nuclear entry of the Notch intracellular domain.Developmental cell · 2024Article
- Structural Requirements for Activity of Mind bomb1 in Notch Signaling.bioRxiv : the preprint server for biology · 2024Article
- Article
- BioE3 identifies specific substrates of ubiquitin E3 ligases.Nature communications · 2023Article
- The meaning of ubiquitylation of the DSL ligand Delta for the development of Drosophila.BMC biology · 2023Article
- SNORA73B promotes endometrial cancer progression through targeting MIB1 and regulating host gene RCC1 alternative splicing.Journal of cellular and molecular medicine · 2023Article
- Tension-tuned receptors for synthetic mechanotransduction and intercellular force detection.Nature biotechnology · 2023Article
- HERC2 promotes inflammation-driven cancer stemness and immune evasion in hepatocellular carcinoma by activating STAT3 pathway.Journal of experimental & clinical cancer research : CR · 2023Article
- In-silico screening and in-vitro assay show the antiviral effect of Indomethacin against SARS-CoV-2.Computers in biology and medicine · 2022Article
- Human Growth Hormone Fragment 176-191 Peptide Enhances the Toxicity of Doxorubicin-Loaded Chitosan Nanoparticles Against MCF-7 Breast Cancer Cells.Drug design, development and therapy · 2022Article
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Mind bomb (Mib) proteins are large, multi-domain E3 ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. This ubiquitination step marks the ligand proteins for epsin-dependent endocytosis, which is critical for in vivo Notch receptor activation. We present here crystal structures of the substrate recognition domains of Mib1, both in isolation and in complex with peptides derived from Notch ligands. The structures, in combination with biochemical, cellular, and in vivo assays, show that Mib1 contains two independent substrate recognition domains that engage two distinct epitopes from the cytoplasmic tail of the ligand Jagged1, one in the intracellular membrane proximal region and the other near the C terminus. Together, these studies provide insights into the mechanism of ubiquitin transfer by Mind bomb E3 ligases, illuminate a key event in ligand-induced activation of Notch receptors, and identify a potential target for therapeutic modulation of Notch signal transduction in disease.
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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.