ArticleMolecular & cellular proteomics : MCP2009
A label-free quantitative proteomics strategy to identify E3 ubiquitin ligase substrates targeted to proteasome degradation.
Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- A guide to mapping ubiquitin and ubiquitin-like E3 ligases to their substrates.The FEBS journal · 2026Review
- A proximity ligation screen identifies SNAT2 as a novel target of the MARCH1 E3 ubiquitin ligase.Biology open · 2026Article
- Fine-tuning levels of filamins a and b as a specific mechanism sustaining Th2 lymphocyte functions.Nature communications · 2024Article
- Identifying E3 Ligase Substrates With Quantitative Degradation Proteomics.Chembiochem : a European journal of chemical biology · 2023Article
- Generation of a CHIP isogenic human iPSC-derived cortical neuron model for functional proteomics.STAR protocols · 2022Article
- A ubiquitin variant-based affinity approach selectively identifies substrates of the ubiquitin ligase E6AP in complex with HPV-11 E6 or HPV-16 E6.The Journal of biological chemistry · 2020Article
- The Role of Cullin-RING Ligases in Striated Muscle Development, Function, and Disease.International journal of molecular sciences · 2020Review
- An Integrative Synthetic Biology Approach to Interrogating Cellular Ubiquitin and Ufm Signaling.International journal of molecular sciences · 2020Article
- Molecular Tuning of Filamin A Activities in the Context of Adhesion and Migration.Frontiers in cell and developmental biology · 2020Review
- Degronomics: Mapping the Interacting Peptidome of a Ubiquitin Ligase Using an Integrative Mass Spectrometry Strategy.Analytical chemistry · 2019Article
- Evaluation of linear models and missing value imputation for the analysis of peptide-centric proteomics.BMC bioinformatics · 2019Article
- The notch pathway promotes NF-κB activation through Asb2 in T cell acute lymphoblastic leukemia cells.Cellular & molecular biology letters · 2018Article
- Systematic approaches to identify E3 ligase substrates.The Biochemical journal · 2016Review
- Proteomics and transcriptomics analyses of Arabidopsis floral buds uncover important functions of ARABIDOPSIS SKP1-LIKE1.BMC plant biology · 2016Article
- Substrates of the ASB2α E3 ubiquitin ligase in dendritic cells.Scientific reports · 2015Article
- Ubiquitin ligase Siah2 regulates RevErbα degradation and the mammalian circadian clock.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Proteomic identification of protein ubiquitination events.Biotechnology & genetic engineering reviews · 2013Review
- Screening E3 substrates using a live phage display library.PloS one · 2013Article
- Label-free quantitative proteomics and N-glycoproteomics analysis of KRAS-activated human bronchial epithelial cells.Molecular & cellular proteomics : MCP · 2012Article
- Quantitative proteomics to decipher ubiquitin signaling.Amino acids · 2012Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ubiquitin-proteasome system is a central mechanism for controlled proteolysis that regulates numerous cellular processes in eukaryotes. As such, defects in this system can contribute to disease pathogenesis. In this pathway, E3 ubiquitin ligases provide platforms for binding specific substrates, thereby coordinating their ubiquitylation and subsequent degradation by the proteasome. Despite the identification of many E3 ubiquitin ligases, the identities of their specific substrates are still largely unresolved. The ankyrin repeat-containing protein with a suppressor of cytokine signaling box 2 (ASB2) gene that we initially identified as a retinoic acid-response gene in acute promyelocytic leukemia cells encodes the specificity subunit of an E3 ubiquitin ligase complex that is involved in hematopoietic cell differentiation. We have recently identified filamin A and filamin B as the first ASB2 targets and shown that ASB2 triggers ubiquitylation and proteasome-mediated degradation of these proteins. Here a global quantitative proteomics strategy is provided to identify substrates of E3 ubiquitin ligases targeted to proteasomal degradation. Indeed we used label-free methods for quantifying proteins identified by shotgun proteomics in extracts of cells expressing wild-type ASB2 or an E3 ubiquitin ligase-defective mutant of ASB2 under the control of an inducible promoter. Measurements of spectral count and mass spectrometric signal intensity demonstrated a drastic decrease of filamin A and filamin B in myeloid leukemia cells expressing wild-type ASB2 compared with cells expressing an E3 ubiquitin ligase-defective mutant of ASB2. Altogether we provide an original strategy that enables identification of E3 ubiquitin ligase substrates that have to be degraded.
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