ArticleMolecular and cellular biology2008
A novel protein, Luman/CREB3 recruitment factor, inhibits Luman activation of the unfolded protein response.
Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 85 citations in OpenAlex.
- Adaptation of the Transcriptome and miRNAome in Response to Hepatocellular Hypoxia.International journal of molecular sciences · 2026Article
- NAA10 and BTRC drive CREBRF degradation in endoplasmic reticulum stress and renal tubular injury.Journal of diabetes investigation · 2026Article
- Beneficially Stressing the Peripheral Nervous System to Repair.International journal of molecular sciences · 2026Review
- Single-cell transcriptomics reveals dynamic reprogramming of testicular immunity inZoological research · 2025Article
- The Unfolded Protein Response-Novel Mechanisms, Challenges, and Key Considerations for Therapeutic Intervention.Cancers · 2025Review
- Targeting CREBRF in Cancer: Mechanistic Insights and Future Directions.Biologics : targets & therapy · 2025Review
- MiR-378 exaggerates angiogenesis and bone erosion in collagen-induced arthritis mice by regulating endoplasmic reticulum stress.Cell death & disease · 2024Article
- CREB3 protein family: the promising therapeutic targets for cardiovascular and metabolic diseases.Cell biology and toxicology · 2024Review
- Dysregulated CREB3 cleavage at the nuclear membrane induces karyoptosis-mediated cell death.Experimental & molecular medicine · 2024Article
- Elucidation of OSW-1-Induced Stress Responses in Neuro2a Cells.International journal of molecular sciences · 2023Article
- Multigenerational mistimed feeding drives circadian reprogramming with an impaired unfolded protein response.Frontiers in endocrinology · 2023Article
- Genetic alterations in CREBRF influence prostate cancer survival and impact prostate tissue homeostasis in mice.American journal of clinical and experimental urology · 2023Article
- Limited Metabolic Effect of the CREBRFCells · 2022Article
- The CREBRF diabetes-protective rs373863828-A allele is associated with enhanced early insulin release in men of Māori and Pacific ancestry.Diabetologia · 2021Article
- Molecular characterization of mouse CREB3 regulatory factor in Neuro2a cells.Molecular biology reports · 2021Article
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- A missense variant in CREBRF is associated with taller stature in Samoans.American journal of human biology : the official journal of the Human Biology Council · 2020Article
- Loss of CREBRF Reduces Anxiety-like Behaviors and Circulating Glucocorticoids in Male and Female Mice.Endocrinology · 2020Article
- Exploring the Paradoxical Relationship of a Creb 3 Regulatory Factor Missense Variant With Body Mass Index and Diabetes Among Samoans: Protocol for the Soifua Manuia (Good Health) Observational Cohort Study.JMIR research protocols · 2020Article
- The UPR in Neurodegenerative Disease: Not Just an Inside Job.Biomolecules · 2020Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Luman/CREB3 (also called LZIP) is an endoplasmic reticulum (ER)-bound cellular transcription factor. It has been implicated in the mammalian unfolded protein response (UPR), as well as herpes simplex virus reactivation from latency in sensory neurons. Here, we report the identification of a novel Luman recruitment factor (LRF). Like Luman, LRF is a UPR-responsive basic-region leucine zipper protein that is prone to proteasomal degradation. Being a highly unstable protein, LRF interacts with Luman through the leucine zipper region and promotes Luman degradation. LRF was found to recruit the nuclear form of Luman to discrete nuclear foci, which overlap with the nuclear receptor coactivator GRIP1 bodies, and repress the transactivation activity of Luman. Compared to LRF+/+ mouse embryonic fibroblast (MEF) cells, the levels of CHOP, EDEM, and Herp were elevated in LRF-/- MEF cells. We propose that LRF is a negative regulator of the UPR. For Luman, it may represent another level of regulation following Luman proteolytic cleavage on the ER and nuclear translocation. In addition to inducing rapid Luman turnover, LRF may repress the transactivation potential of Luman by sequestering it in the LRF nuclear bodies away from key cofactors (such as HCF-1) that are required for transcriptional activation.
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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.