ArticleeLife2016
DPP9 is a novel component of the N-end rule pathway targeting the tyrosine kinase Syk.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 58 citations in OpenAlex.
- Caspase-mediated cleavage events hidden by secondary proteolysis during apoptosis.Protein science : a publication of the Protein Society · 2026Article
- A C-degron regulates Chk1 kinase by allowing stability of inactive Chk1 and by making it short- lived upon activation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Proximity labeling reveals non-catalytic interactions between DPP9 and ubiquitin signaling complexes.Cellular and molecular life sciences : CMLS · 2026Article
- Reduced DPP9 levels sensitize experimental breast tumors to combinatory treatment with irradiation and Olaparib.Frontiers in oncology · 2026Article
- A Photocaged N-Phosphonopiperidinone as a Selective Photo-Cleavable DPP8/9 Inhibitor.Chembiochem : a European journal of chemical biology · 2025Article
- A fluorescent sensor for real-time monitoring of DPP8/9 reveals crucial roles in immunity and cancer.Life science alliance · 2025Article
- Hippocampal dipeptidyl peptidase 9 bidirectionally regulates memory associated with synaptic plasticity.Journal of advanced research · 2025Article
- The multifunctional regulatory post-proline protease dipeptidyl peptidase 9 and its inhibitors: new opportunities for therapeutics.Cellular and molecular life sciences : CMLS · 2025Review
- The serine protease DPP9 and the redox sensor KEAP1 form a mutually inhibitory complex.The Journal of biological chemistry · 2025Article
- N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024Review
- DPP9 regulates NQO1 and ROS to promote resistance to chemotherapy in liver cancer cells.Redox biology · 2024Article
- Dipeptidyl peptidases and E3 ligases of N-degron pathways cooperate to regulate protein stability.The Journal of cell biology · 2024Article
- Development of the dipeptidyl peptidase 4 family and its association with lung diseases: a narrative review.Journal of thoracic disease · 2023Review
- Dipeptidyl-Aminopeptidases 8 and 9 Regulate Autophagy and Tamoxifen Response in Breast Cancer Cells.Cells · 2023Article
- Article
- DPP8/9 are not Required to Cleave Most Proline-Containing Peptides.Israel journal of chemistry · 2023Article
- Chemoproteomics-Enabled Identification of 4-Oxo-β-Lactams as Inhibitors of Dipeptidyl Peptidases 8 and 9.Angewandte Chemie (International ed. in English) · 2022Article
- Dipeptidyl peptidase 9 triggers BRCA2 degradation and promotes DNA damage repair.EMBO reports · 2022Article
- DPP9 deficiency: An inflammasomopathy that can be rescued by lowering NLRP1/IL-1 signaling.Science immunology · 2022Article
- Crystal structure of the Ate1 arginyl-tRNA-protein transferase and arginylation of N-degron substrates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aminopeptidase DPP9 removes dipeptides from N-termini of substrates having a proline or alanine in second position. Although linked to several pathways including cell survival and metabolism, the molecular mechanisms underlying these outcomes are poorly understood. We identified a novel interaction of DPP9 with Filamin A, which recruits DPP9 to Syk, a central kinase in B-cell signalling. Syk signalling can be terminated by degradation, requiring the ubiquitin E3 ligase Cbl. We show that DPP9 cleaves Syk to produce a neo N-terminus with serine in position 1. Pulse-chases combined with mutagenesis studies reveal that Ser1 strongly influences Syk stability. Furthermore, DPP9 silencing reduces Cbl interaction with Syk, suggesting that DPP9 processing is a prerequisite for Syk ubiquitination. Consistently, DPP9 inhibition stabilizes Syk, thereby modulating Syk signalling. Taken together, we demonstrate DPP9 as a negative regulator of Syk and conclude that DPP9 is a novel integral aminopeptidase of the N-end rule pathway.
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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.