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.[7]
Lamin B receptor has been shown to interact with CBX3[10] and CBX5.[10] LBR also interacts with long non-coding RNAXIST in mouse cells and potentially assist the spreading XIST across X chromosome in differentiating female embryonic stem cells,[11] but it might be redundant for correct XCI in vivo.[12]
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Papoutsopoulou S, Nikolakaki E, Giannakouros T (February 1999). "SRPK1 and LBR protein kinases show identical substrate specificities". Biochemical and Biophysical Research Communications. 255 (3): 602–7. doi:10.1006/bbrc.1999.0249. PMID10049757.
Hoffmann K, Dreger CK, Olins AL, Olins DE, Shultz LD, Lucke B, Karl H, Kaps R, Müller D, Vayá A, Aznar J, Ware RE, Sotelo Cruz N, Lindner TH, Herrmann H, Reis A, Sperling K (August 2002). "Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huët anomaly)". Nature Genetics. 31 (4): 410–4. doi:10.1038/ng925. PMID12118250. S2CID6020153.
