ArticleThe Journal of biological chemistry2019
SDF2-like protein 1 (SDF2L1) regulates the endoplasmic reticulum localization and chaperone activity of ERdj3 protein.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 50 citations in OpenAlex.
- Article
- SDF2L1 modulates oxLDL-induced endoplasmic reticulum stress, protein aggregation, and O-mannosylation in myocardial infarction and lung cancer.Cellular and molecular life sciences : CMLS · 2026Article
- Effects of miR-210-3p/SDF2 and miR-31-5p/FGF7 from hypoxic endometrial exosomes on UCB-MSC proliferation, migration, and differentiation.Stem cell research & therapy · 2025Article
- SDF2 promotes glioma progression via GRP78‑mediated ERAD and copper homeostasis disruption.International journal of molecular medicine · 2025Article
- Sex-Specific Effects of Early-Life Stress Exposure on Memory Performance and the Medial Prefrontal Cortex Transcriptomic Pattern in Adolescent Mice.Molecular neurobiology · 2025Article
- Identifying Pyroptosis-Hub Genes and Inflammation Cell Type-Related Genes in Ischemic Stroke.Molecular neurobiology · 2025Article
- High Glucose-induced transcriptomic changes in human trabecular meshwork cells.Molecular biology reports · 2025Article
- UBE2J1 is identified as a novel plasma cell-related gene involved in the prognosis of high-grade serous ovarian cancer.Journal of translational medicine · 2025Article
- Suppression of melanoma by mice lacking MHC-II: Mechanisms and implications for cancer immunotherapy.The Journal of experimental medicine · 2024Article
- Turnover of EDEM1, an ERAD-enhancing factor, is mediated by multiple degradation routes.Genes to cells : devoted to molecular & cellular mechanisms · 2024Article
- ATM-mediated co-chaperone DNAJB11 phosphorylation facilitates α-synuclein folding upon DNA double-stranded breaks.NAR molecular medicine · 2024Article
- Simultaneous proteome localization and turnover analysis reveals spatiotemporal features of protein homeostasis disruptions.Nature communications · 2024Article
- Simultaneous proteome localization and turnover analysis reveals spatiotemporal features of protein homeostasis disruptions.bioRxiv : the preprint server for biology · 2024Article
- Dysregulated UPR and ER Stress Related to a Mutation in theInternational journal of molecular sciences · 2023Article
- Gene expression networks and functionally enriched pathways involved in the response of domestic chicken to acute heat stress.Frontiers in genetics · 2023Article
- Article
- Large-scale sequencing identifies multiple genes and rare variants associated with Crohn's disease susceptibility.Nature genetics · 2022Article
- Regulation of Translation, Translocation, and Degradation of Proteins at the Membrane of the Endoplasmic Reticulum.International journal of molecular sciences · 2022Review
- St13 protects against disordered acinar cell arachidonic acid pathway in chronic pancreatitis.Journal of translational medicine · 2022Article
- Stress-responsive regulation of extracellular proteostasis.The Journal of cell biology · 2022Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular chaperones facilitate protein folding by associating with nascent polypeptides, thereby preventing protein misfolding and aggregation. Endoplasmic reticulum (ER) chaperone BiP, the sole HSP70 chaperone in the ER, is regulated by HSP40 chaperones, including ER-resident protein ERdj3 (DNAJB11). ERdj3 lacks an ER retrieval signal, is secreted under ER stress conditions, and functions as a chaperone in the extracellular space, but how its secretion is regulated remains unclear. We recently showed that ERdj3 forms a complex with ER-resident stromal cell-derived factor 2 (SDF2) and SDF2L1 (SDF2-like protein 1) and thereby prevents protein aggregation during the BiP chaperone cycle. However, the contribution of the ERdj3-SDF2L1 complex to protein quality control is poorly understood. Here, we analyzed the intracellular localization and chaperone activity of ERdj3 in complex with SDF2L1. We found that ERdj3 was retained in the ER by associating with SDF2/SDF2L1.
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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.