ArticleNature communications2019
Ufbp1 promotes plasma cell development and ER expansion by modulating distinct branches of UPR.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 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.
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Who cites it
66 citing papers in PubMed, 114 citations in OpenAlex.
- Ubiquitin and ubiquitin-like modifications in the endoplasmic reticulum stress response.The FEBS journal · 2026Review
- Narrative review-the emerging role, functions, and mechanisms of UFMylation in cancers.Translational cancer research · 2026Review
- Identification and Experimental Validation of Key Genes Related to Neuroendocrine in Periodontitis Based on Single-Cell and Bulk Transcriptome Data.Journal of cellular and molecular medicine · 2026Article
- The UFSP2-C1orf27 complex positions nascent GPCRs to the ufmylation system for ER export control.iScience · 2026Article
- Ufmylation-Deficient DDRGK1 Ameliorates Obesity by Inhibiting FASN-Mediated Adipocyte Lipogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- A genus-wide interaction atlas across NS4B orthologues identifies a conserved role for UFMylation in orthoflavivirus replication.Nature communications · 2026Article
- The UFM1 Conjugation System: A Master Regulator of Cellular Stress Surveillance in Human Disease.Biology · 2026Review
- DDRGK1 preserves intervertebral disc development through ufmylation.Cellular and molecular life sciences : CMLS · 2025Article
- Multi-omics profiling reveals an immunosuppressive plasma cell subset within tertiary lymphoid structures in cervical cancer.Cancer immunology, immunotherapy : CII · 2025Article
- UFM1 at the endoplasmic reticulum: linking ER stress, ribosome quality control, and ER-phagy.Essays in biochemistry · 2025Review
- Role of hyperhomocysteinemia in atherosclerosis: from bench to bedside.Annals of medicine · 2025Review
- UFMylation: A supervisor of the HIF1α pathway and a potential therapeutic target for anti-PD-1 combination therapy in hypoxic tumors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Relationship between plasma homocysteine and clinical grading of varicocele.Asian journal of andrology · 2025Article
- Studies on the functional role of UFMylation in cells (Review).Molecular medicine reports · 2025Review
- Control of Rhizobia Endosymbiosis by Coupling ER Expansion with Enhanced UPR.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Multifaceted roles of UFMylation in health and disease.Acta pharmacologica Sinica · 2025Review
- UFL1 promotes survival and function of virtual memory CD8 T cells.Journal of immunology (Baltimore, Md. : 1950) · 2025Article
- The emerging roles of UFMylation in the modulation of immune responses.Clinical and translational medicine · 2024Review
- The ufmylation cascade controls COPII recruitment, anterograde transport, and sorting of nascent GPCRs at ER.Science advances · 2024Article
- Post-translational modifications: emerging directors of cell-fate decisions during endoplasmic reticulum stress in Arabidopsis thaliana.Biochemical Society transactions · 2024Review
6 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
The IRE1α/XBP1 branch of unfolded protein response (UPR) pathway has a critical function in endoplasmic reticulum (ER) expansion in plasma cells via unknown mechanisms; interestingly, another UPR branch, PERK, is suppressed during plasma cell development. Here we show that Ufbp1, a target and cofactor of the ufmylation pathway, promotes plasma cell development by suppressing the activation of PERK. By contrast, the IRE1α/XBP1 axis upregulates the expression of Ufbp1 and ufmylation pathway genes in plasma cells, while Ufbp1 deficiency impairs ER expansion in plasma cells and retards immunoglobulin production. Structure and function analysis suggests that lysine 267 of Ufbp1, the main lysine in Ufbp1 that undergoes ufmylation, is dispensable for the development of plasmablasts, but is required for immunoglobulin production and stimulation of ER expansion in IRE1α-deficient plasmablasts. Thus, Ufbp1 distinctly regulates different branches of UPR pathway to promote plasma cell development and function.
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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.