LBR
GeneName
LBR
Summary
LBR, also known as lamin B receptor or dLBR, is a 71 kDa integral membrane protein primarily located in the nuclear envelope and endoplasmic reticulum membrane. It plays a role in chromatin organisation and is involved in the binding of lamin proteins, which are essential for maintaining nuclear structure. LBR also participates in various cellular processes, including cholesterol biosynthesis and the differentiation of neutrophils. Its ability to bind DNA and RNA suggests a role in gene regulation and chromatin dynamics, while its presence in the nucleoplasm and cytoplasm indicates multifunctional properties within the cell.
Importance
LBR is relevant to: - The regulation of nuclear architecture and chromatin organisation, impacting gene expression and cellular function - Cholesterol metabolism, which is crucial for membrane integrity and cellular signalling - Neutrophil differentiation, influencing immune responses and inflammation - The random inactivation of the X chromosome, which is important for understanding dosage compensation in female mammals
Top Products
For researchers investigating LBR, we highly recommend the top-selling recombinant antibody, Anti-Lamin B Receptor/LBR antibody [E398L] (ab32535). This antibody has been validated in knockout models and is suitable for a variety of applications, including Western blotting (WB), immunocytochemistry (ICC), immunohistochemistry (IHC), and flow cytometry (FC). With 66 citations, it has garnered significant attention in the research community, reflecting its reliability and effectiveness in detecting LBR. This product is an excellent choice for those seeking consistent and robust results in their studies.
Abcam Product Citation Summary
The data indicates that the Abcam antibody ab32535 has been employed in Western Blot experiments to detect LBR in human samples. This suggests a focus on understanding the role of LBR in human biology or disease contexts.
Abcam Product Citation Table
Domain
The Tudor domain may not recognize methylation marks, but rather bind unassembled free histone H3.
Function
Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (PubMed:12618959, PubMed:16784888, PubMed:21327084, PubMed:27336722, PubMed:9630650). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (PubMed:10828963).
Involvement in disease
Pelger-Huet anomaly
PHA
An autosomal dominant inherited abnormality of granulocytes, characterized by abnormal ovoid shape, reduced nuclear segmentation and an apparently looser chromatin structure.
None
The disease is caused by variants affecting the gene represented in this entry.
Greenberg dysplasia
GRBGD
A rare autosomal recessive chondrodystrophy characterized by early in utero lethality. Affected fetuses typically present with fetal hydrops, short-limbed dwarfism, and a marked disorganization of chondro-osseous calcification, and ectopic ossification centers.
None
The disease is caused by variants affecting the gene represented in this entry.
Reynolds syndrome
REYNS
A syndrome specifically associating limited cutaneous systemic sclerosis and primary biliary cirrhosis. It is characterized by liver disease, telangiectasia, abrupt onset of digital paleness or cyanosis in response to cold exposure or stress (Raynaud phenomenon), and variable features of scleroderma. The liver disease is characterized by pruritis, jaundice, hepatomegaly, increased serum alkaline phosphatase and positive serum mitochondrial autoantibodies, all consistent with primary biliary cirrhosis.
None
The disease may be caused by variants affecting the gene represented in this entry.
Rhizomelic skeletal dysplasia with or without Pelger-Huet anomaly
SKPHA
A disease characterized by abnormal nuclear shape and chromatin organization in blood granulocytes, short stature, and mild skeletal anomalies. Initial skeletal features may improve with age.
None
The disease is caused by variants affecting the gene represented in this entry.
Pathway
Steroid biosynthesis; cholesterol biosynthesis.
Post-translational modifications
Phosphorylated by CDK1 in mitosis when the inner nuclear membrane breaks down into vesicles that dissociate from the lamina and the chromatin. It is phosphorylated by different protein kinases in interphase when the membrane is associated with these structures. Phosphorylation of LBR and HP1 proteins may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle. Phosphorylated by SRPK1. In late anaphase LBR is dephosphorylated, probably by PP1 and/or PP2A, allowing reassociation with chromatin.
Sequence Similarities
Belongs to the ERG4/ERG24 family.
Tissue Specificity
Expressed in the bone marrow, liver, heart, adrenal gland, lung, placenta and uterus (PubMed:16784888). Expressed in osteoclasts and osteoblast-like cells (PubMed:21327084).
Cellular localization
- Nucleus inner membrane
- Multi-pass membrane protein
- Endoplasmic reticulum membrane
- Cytoplasm
- Nucleus
- Nucleus; nuclear rim.
Alternative names
Delta(14)-sterol reductase LBR, Delta-14-SR, 3-beta-hydroxysterol Delta (14)-reductase, C-14 sterol reductase, Integral nuclear envelope inner membrane protein, LMN2R, Lamin-B receptor, Sterol C14-reductase, C14SR, LBR