ArticleeLife2016
The Lamin B receptor is essential for cholesterol synthesis and perturbed by disease-causing mutations.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
What it found
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Who cites it
68 citing papers in PubMed, 101 citations in OpenAlex.
- A homozygous lamin B receptor variant resulting in Pelger-Huët anomaly without skeletal dysplasia.Nucleus (Austin, Tex.) · 2026Article
- Nuclear mechanobiology rules immune cells' functions: from differentiation to cell trafficking and pathogen killing.Nucleus (Austin, Tex.) · 2026Review
- Nuclear envelope rupture and resealing: mechanisms, consequences, and disease implications.Biochemical Society transactions · 2026Review
- Diet-responsive proteogenomic effects following short-term restriction of animal products in humans.Nature communications · 2026Article
- A sterol reductase responsible for the unusual 8(14)-unsaturation in bacterial sterol production and degradation.Journal of bacteriology · 2026Article
- Review
- A sterol reductase responsible for the unusual 8(14)-unsaturation in bacterial sterol production and degradation.bioRxiv : the preprint server for biology · 2026Article
- Lamin B receptor upregulation in metastatic melanoma causes nuclear envelope fragility in confined migration during cancer invasion.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Cholesterol Metabolism: An Ally in the Development and Progression of Cervical Cancer.International journal of molecular sciences · 2026Review
- The Inner Nuclear Membrane Has a Unique Lipid Signature.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Nuclear cholesterol regulates nuclear size and DNA damage responses in cancer stem cells.Neuro-oncology · 2025Article
- Mutation of Brain Aromatase Impairs Behavior and Neuroplasticity in Adult Zebrafish.Journal of neurochemistry · 2025Article
- Nondisruptive inducible labeling of ER-membrane contact sites using the Lamin B receptor.PLoS biology · 2025Article
- SHMT2 is essential for mammalian preimplantation embryonic development throughMolecular therapy. Nucleic acids · 2025Article
- Neutrophils secrete exosome-associated DNA to resolve sterile acute inflammation.Nature cell biology · 2025Article
- A quantitative ultrastructural timeline of nuclear autophagy reveals a role for dynamin-like protein 1 at the nuclear envelope.Nature cell biology · 2025Article
- Novel lamin B receptor mutation (c.561C > G) in a patient with Pelger-Huët anomaly: a case report.Frontiers in pediatrics · 2025Article
- LAP1 Interactome Profiling Provides New Insights into LAP1's Physiological Functions.International journal of molecular sciences · 2024Article
- A quantitative ultrastructural timeline of nuclear autophagy reveals a role for dynamin-like protein 1 at the nuclear envelope.bioRxiv : the preprint server for biology · 2024Article
- Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Lamin B receptor (LBR) is a polytopic membrane protein residing in the inner nuclear membrane in association with the nuclear lamina. We demonstrate that human LBR is essential for cholesterol synthesis. LBR mutant derivatives implicated in Greenberg skeletal dysplasia or Pelger-Huët anomaly fail to rescue the cholesterol auxotrophy of a LBR-deficient human cell line, consistent with a loss-of-function mechanism for these congenital disorders. These disease-causing variants fall into two classes: point mutations in the sterol reductase domain perturb enzymatic activity by reducing the affinity for the essential cofactor NADPH, while LBR truncations render the mutant protein metabolically unstable, leading to its rapid degradation at the inner nuclear membrane. Thus, metabolically unstable LBR variants may serve as long-sought-after model substrates enabling previously impossible investigations of poorly understood protein turnover mechanisms at the inner nuclear membrane of higher eukaryotes.
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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.