Lamin B receptor

Olins, Ada L.; Rhodes, Gale; Welch, David; Zwerger, Monika; Olins, Donald E.

doi:10.4161/nucl.1.1.10515

Cited by 140 publications

(118 citation statements)

References 142 publications

(204 reference statements)

Supporting

Mentioning

111

Contrasting

Order By: Relevance

“…Certainly, at this point and in the lack of sound experimental evidence, this is only a hypothesis and needs to be validated in a concrete biological context. However, this hypothesis highlights an alternative scenario for the functional role of LBR in the nuclear envelope, which remains elusive, despite its experimentally documented association with chromatin and nuclear lamina (26). This scenario is compatible with the presumed role of nuclear envelope as a platform for peripheral heterochromatin assembly and chromatin remodeling, based on a large body of experimental evidence (24 -27).…”

Section: Discussionsupporting

confidence: 49%

Solution Structure and Molecular Interactions of Lamin B Receptor Tudor Domain

Liokatis

Edlich

Soupsana

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Lamin B receptor (LBR) is an integral nuclear envelope protein and contains a Tudor domain. Results:The NMR structure of LBR-Tudor was determined and its interactions with nuclear proteins, histones, and nucleosomes were explored. Conclusion: LBR-Tudor is not involved in recognition of methylated histones and binds free H3. Significance: Tudor domains may act as histone chaperone-like platforms.

show abstract

Section: Discussionsupporting

confidence: 49%

Solution Structure and Molecular Interactions of Lamin B Receptor Tudor Domain

Liokatis

Edlich

Soupsana

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…LBR also interacts with heterochromatin, and is believed to have a key role in the normal distribution of chromatin within the post-mitotic nucleus. In addition to lamin proteins and DNA, LBR has large number of downstream effectors, believed to impact the cell cycle [29] and has a negative role in cellular differentiation [6]. Defects in LBR have been implicated in a hematological condition known as the Pelger-Huët anomaly.…”

Section: Discussionmentioning

confidence: 99%

The clinicopathological significance of lamin A/C, lamin B1 and lamin B receptor mRNA expression in human breast cancer

Wazir¹,

Ahmed²,

Bridger³

et al. 2013

Cellular and Molecular Biology Letters

View full text Add to dashboard Cite

Lamin A/C (LMNA), lamin B1 (LMNB1) and lamin B receptor (LBR) have key roles in nuclear structural integrity and chromosomal stability. In this study, we have studied the relationships between the mRNA expressions of A-type lamins, LMNB1 and LBR and the clinicopathological parameters in human breast cancer. Samples of breast cancer tissues (n = 115) and associated non-cancerous tissue (ANCT; n = 30) were assessed using reverse transcription and quantitative PCR. Transcript levels were correlated with clinicopathological data. Higher levels of A-type lamins and LMNB1 mRNA expression were seen in ANCT. Higher lamin A/C expression was associated with the early clinical stage (TNM1 vs. TNM3 — 13 vs. 0.21; p = 0.0515), with better clinical outcomes (disease-free survival vs. mortality — 11 vs. 1; p = 0.0326), and with better overall (p = 0.004) and disease-free survival (p = 0.062). The expression of LMNB1 declined with worsening clinical outcome (disease-free vs. mortalities — 0.0011 vs. 0.000; p = 0.0177). LBR mRNA expression was directly associated with tumor grade (grade 1 vs. grade 3 — 0.00 vs. 0.00; p = 0.0479) and Nottingham Prognostic Index (NPI1 vs. NPI3 — 0.00 vs. 0.00; p = 0.0551). To the best of our knowledge, this is the first study to suggest such a role for A-type lamins, lamin B1 and LBR in human breast cancer, identifying an important area for further research.

show abstract

“…Furthermore, it is suggested that this function (maintaining nuclear architecture throughout the cell cycle) has been highly conserved by evolution. Epichromatin could affect post-mitotic nuclear reformation by presenting preferred interaction sites for early-binding nuclear envelope integral membrane proteins (e.g., LBR and LAP2β 21,22,37 ). In a "deterministic" version of the epichromatin hypothesis, this attractive chromatin conformation is always located at the same regions of specific chromosomes, ensuring that these chromosome regions have preferred positions adjacent to the nuclear envelope during post-mitotic nuclear reformation.…”

Section: Discussionmentioning

confidence: 99%

An epichromatin epitope: Persistence in the cell cycle and conservation in evolution

Olins¹,

Langhans²,

Monestier³

et al. 2011

nucleus

Self Cite

View full text Add to dashboard Cite

NucleusVolume 2 Issue 1 U2OS and HL-60/S4 cells by deconvolution immunofluorescence microscopy with the aim of searching for chromatin substructures. One anti-nucleosome antibody (PL2-6) specifically stained a chromatin compartment at the periphery of interphase nuclei, as well as staining the surface of mitotic chromosomes. We suggest that this compartment represents a unique surface chromatin conformation, to which we assign the name "epichromatin". Furthermore, we formulate an "epichromatin hypothesis", suggesting that this chromatin may play a crucial role in organizing interphase nuclear architecture, justifying its conservation in the evolution of cell structure. Results

show abstract

Lamin B receptor

Cited by 140 publications

References 142 publications

Solution Structure and Molecular Interactions of Lamin B Receptor Tudor Domain

Solution Structure and Molecular Interactions of Lamin B Receptor Tudor Domain

The clinicopathological significance of lamin A/C, lamin B1 and lamin B receptor mRNA expression in human breast cancer

An epichromatin epitope: Persistence in the cell cycle and conservation in evolution

Contact Info

Product

Resources

About