ArticlePloS one2017
Dynamics and Structure-Function Relationships of the Lamin B Receptor (LBR).
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Envelope-Limited Chromatin Sheets (ELCS) Formation in The Nuclear Envelope of HL-60/S4 Cells.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
- Spatial proteomics of ER tubules reveals CLMN, an ER-actin tether at focal adhesions that promotes cell migration.Cell reports · 2025Article
- Spatial proteomics of ER tubules reveals CLMN, an ER-actin tether at focal adhesions that promotes cell migration.bioRxiv : the preprint server for biology · 2024Article
- Shared and Distinctive Neighborhoods of Emerin and Lamin B Receptor Revealed by Proximity Labeling and Quantitative Proteomics.Journal of proteome research · 2022Article
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- Small heat-shock protein HSPB3 promotes myogenesis by regulating the lamin B receptor.Cell death & disease · 2021Article
- Deletion of LBR N-terminal domains recapitulates Pelger-Huet anomaly phenotypes in mouse without disrupting X chromosome inactivation.Communications biology · 2021Article
- The PRR14 heterochromatin tether encodes modular domains that mediate and regulate nuclear lamina targeting.Journal of cell science · 2020Article
- Characterization of lamin B receptor of Sf9 cells and its fate during Autographa californica nucleopolyhedrovirus infection.Cytotechnology · 2020Article
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- Article
- The Neutrophil Nucleus: An Important Influence on Neutrophil Migration and Function.Frontiers in immunology · 2018Review
- Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lamin B receptor (LBR) is a multi-spanning membrane protein of the inner nuclear membrane that is often employed as a "reporter" of nuclear envelope dynamics. We show here that the diffusional mobility of full-length LBR exhibits significant regional variation along the nuclear envelope, consistent with the existence of discrete LBR microdomains and the occurrence of multiple, asymmetrically-spaced anastomoses along the nuclear envelope-endoplasmic reticulum interface. Interestingly, a commonly used fusion protein that contains the amino-terminal region and the first transmembrane domain of LBR exhibits reduced mobility at the nuclear envelope, but behaves similarly to full-length LBR in the endoplasmic reticulum. On the other hand, carboxy-terminally truncated mutants that retain the first four transmembrane domains and a part or the whole of the amino-terminal region of LBR are generally hyper-mobile. These results suggest that LBR dynamics is structure and compartment specific. They also indicate that native LBR is probably "configured" by long-range interactions that involve the loops between adjacent transmembrane domains and parts of the amino-terminal region.
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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.