Biology:Lamin B receptor

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Lamin-B receptor is a protein, and in humans, it is encoded by the LBR gene.[1][2][3]

Function

The protein encoded by this gene belongs to the ERG4/ERG24 family. It localizes to the inner membrane of the nuclear envelope and anchors the lamina and the heterochromatin to the membrane. It may mediate the interaction between chromatin and lamin B. Mutations of this gene has been associated with autosomal recessive HEM/Greenberg skeletal dysplasia. Alternative splicing occurs at this locus and two transcript variants encoding the same protein have been identified.[3]

Clinical significance

There is evidence tying it to Greenberg dysplasia[4] and Pelger-Huet anomaly.[5]

Interactions

Lamin B receptor has been shown to interact with CBX3[6] and CBX5.[6] LBR also interacts with long non-coding RNA XIST in mouse cells and potentially assist the spreading XIST across X chromosome in differentiating female embryonic stem cells,[7] but it might be redundant for correct XCI in vivo.[8]

References

  1. "Characterization of the human gene encoding LBR, an integral protein of the nuclear envelope inner membrane". The Journal of Biological Chemistry 269 (15): 11312–7. April 1994. doi:10.1016/S0021-9258(19)78127-7. PMID 8157663. 
  2. "The human lamin B receptor/sterol reductase multigene family". Genomics 54 (3): 469–76. December 1998. doi:10.1006/geno.1998.5615. PMID 9878250. 
  3. 3.0 3.1 "Entrez Gene: LBR lamin B receptor". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3930. 
  4. Online Mendelian Inheritance in Man (OMIM) 215140
  5. Online Mendelian Inheritance in Man (OMIM) 169400
  6. 6.0 6.1 "Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1". The Journal of Biological Chemistry 271 (25): 14653–6. June 1996. doi:10.1074/jbc.271.25.14653. PMID 8663349. 
  7. "Xist recruits the X chromosome to the nuclear lamina to enable chromosome-wide silencing". Science 354 (6311): 468–472. October 2016. doi:10.1126/science.aae0047. PMID 27492478. Bibcode2016Sci...354..468C. 
  8. Young, Alexander Neil; Perlas, Emerald; Ruiz-Blanes, Nerea; Hierholzer, Andreas; Pomella, Nicola; Martin-Martin, Belen; Liverziani, Alessandra; Jachowicz, Joanna W. et al. (2021-04-12). "Deletion of LBR N-terminal domains recapitulates Pelger-Huet anomaly phenotypes in mouse without disrupting X chromosome inactivation". Communications Biology 4 (1): 478. doi:10.1038/s42003-021-01944-2. ISSN 2399-3642. PMID 33846535. PMC 8041748. http://dx.doi.org/10.1038/s42003-021-01944-2. 

Further reading

External links