ArticleThe Journal of cell biology1990
The lamin B receptor of the nuclear envelope inner membrane: a polytopic protein with eight potential transmembrane domains.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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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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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
58 citing papers in PubMed, 235 citations in OpenAlex.
- Dysregulation of cellular membrane homeostasis as a crucial modulator of cancer risk.The FEBS journal · 2024Review
- Molecular Pathology of Laminopathies.Annual review of pathology · 2022Review
- Regulation of ER Composition and Extent, and Putative Action in Protein Networks by ER/NE Protein TMEM147.International journal of molecular sciences · 2021Article
- Review
- Characterization of lamin B receptor of Sf9 cells and its fate during Autographa californica nucleopolyhedrovirus infection.Cytotechnology · 2020Article
- Casting a Wider Net: Differentiating between Inner Nuclear Envelope and Outer Nuclear Envelope Transmembrane Proteins.International journal of molecular sciences · 2019Review
- Subcellular localization of sterol biosynthesis enzymes.Journal of molecular histology · 2019Article
- A common pathomechanism in GMAP-210- and LBR-related diseases.JCI insight · 2018Article
- Mechanisms of allelic and clinical heterogeneity of lamin A/C phenotypes.Physiological genomics · 2018Review
- Article
- The Lamin B receptor is essential for cholesterol synthesis and perturbed by disease-causing mutations.eLife · 2016Article
- Pelger-Huët anomaly and Greenberg skeletal dysplasia: LBR-associated diseases of cholesterol metabolism.Rare diseases (Austin, Tex.) · 2016Article
- Lamina-associated polypeptide 1: protein interactions and tissue-selective functions.Seminars in cell & developmental biology · 2014Review
- Spatial localization of genes determined by intranuclear DNA fragmentation with the fusion proteins lamin KRED and histone KRED und visible light.International journal of medical sciences · 2013Article
- Inner nuclear membrane proteins: impact on human disease.Chromosoma · 2012Review
- Requirement for lamin B receptor and its regulation by importin {beta} and phosphorylation in nuclear envelope assembly during mitotic exit.The Journal of biological chemistry · 2010Article
- Lamin-binding Proteins.Cold Spring Harbor perspectives in biology · 2010Review
- Diseases of the nuclear envelope.Cold Spring Harbor perspectives in biology · 2010Review
- Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin.Genes & development · 2008Review
- Evaluation of mammalian cell-free systems of nuclear disassembly and assembly.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The lamin B receptor is a previously identified integral membrane protein in the nuclear envelope of turkey erythrocytes that associates with the nuclear intermediate filament protein lamin B (Worman, H. J., J. Yuan, G. Blobel, and S. D. Georgatos. 1988. Proc. Natl. Acad. Sci. USA. 85:8531-8534). In the present report, we use cell fractionation and antibodies against the lamin B receptor to localize it to an 8-M urea-extracted membrane fraction of chicken liver nuclei, supporting an inner nuclear membrane localization. We deduced the amino acid sequence of the chicken lamin B receptor from overlapping clones obtained by screening cDNA libraries with a probe generated by the polymerase chain reaction with primers based on the partial protein sequence of the isolated protein. The mature lamin B receptor has a calculated molecular mass of 73,375 D and eight segments of hydrophobic amino acids that could function as transmembrane domains as determined by hydropathy analysis. Preceding the first putative transmembrane segment is a highly charged 204-residue-long amino terminal region that contains two consensus sites for phosphorylation by protein kinase A. Since the lamin B receptor has been shown to be phosphorylated by protein kinase A in vitro and in vivo and this phosphorylation affects lamin B binding (Applebaum, J., G. Blobel, and S. D. Georgatos. 1990. J. Biol. Chem. 265:4181-4185), it is likely that this amino terminal region faces the nucleoplasm. The amino terminal region also contains three DNA-binding motifs that are found in gene regulatory proteins and histones, suggesting that the lamin B receptor may additionally play a role in gene regulation and/or chromatin organization.
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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.