Structural organization of the human gene (LMNB1) encoding nuclear lamin B1
- PMID: 7557986
- DOI: 10.1006/geno.1995.1036
Structural organization of the human gene (LMNB1) encoding nuclear lamin B1
Abstract
We have determined the structural organization of the human gene (LMNB1) that encodes nuclear lamin B1, an intermediate filament protein of the nuclear envelope. The transcription unit spans more than 45 kb and the transcription start site is 348 nucleotides upstream from the translation initiation codon. Lamin B1 is encoded by 11 exons. Exon 1 codes for the amino-terminal head domain and the first portion of the central rod domain, exons 2 through 6 the central rod domain, and exons 7 through 11 the carboxyl-terminal tail domain of this intermediate filament protein. Intron positions are conserved in other lamin genes from frogs, mice, and humans but different in lamin genes from Drosophila melanogaster and Caenorhabditis elegans. In the region encoding the central rod domain, intron positions are also similar to those in the gene for an invertebrate nonneuronal cytoplasmic intermediate filament protein and the genes for most vertebrate cytoplasmic intermediate filament proteins except neurofilaments and nestin.
Similar articles
-
Genomic structure of the mouse gene (Lmnb1) encoding nuclear lamin B1.Genomics. 1995 Nov 20;30(2):342-6. doi: 10.1006/geno.1995.9868. Genomics. 1995. PMID: 8586436
-
In contrast to the nematode and fruit fly all 9 intron positions of the sea anemone lamin gene are conserved in human lamin genes.Eur J Cell Biol. 2008 May;87(5):305-9. doi: 10.1016/j.ejcb.2008.01.003. Epub 2008 Mar 6. Eur J Cell Biol. 2008. PMID: 18328593
-
Gene structure and chromosomal localization of the murine lamin B2 gene.Eur J Cell Biol. 1991 Dec;56(2):342-50. Eur J Cell Biol. 1991. PMID: 1802718
-
Aspects of the evolution of the lamin/intermediate filament protein family: a current analysis of invertebrate intermediate filament proteins.Biochem Soc Trans. 1991 Nov;19(4):1021-3. doi: 10.1042/bst0191021. Biochem Soc Trans. 1991. PMID: 1794458 Review. No abstract available.
-
Evolution of the lamin protein family: what introns can tell.Nucleus. 2012 Jan-Feb;3(1):44-59. doi: 10.4161/nucl.18927. Nucleus. 2012. PMID: 22156746 Review.
Cited by
-
Interdependent changes of nuclear lamins, nuclear pore complexes, and ploidy regulate cellular regeneration and stress response in the heart.Nucleus. 2023 Dec;14(1):2246310. doi: 10.1080/19491034.2023.2246310. Nucleus. 2023. PMID: 37606283 Free PMC article. Review.
-
Nuclear lamins and laminopathies.J Pathol. 2012 Jan;226(2):316-25. doi: 10.1002/path.2999. Epub 2011 Nov 14. J Pathol. 2012. PMID: 21953297 Free PMC article. Review.
-
Roles of the lamin A-specific tail region in the localization to sites of nuclear envelope rupture.PNAS Nexus. 2024 Nov 21;3(12):pgae527. doi: 10.1093/pnasnexus/pgae527. eCollection 2024 Dec. PNAS Nexus. 2024. PMID: 39677369 Free PMC article.
-
Nuclear envelope: a new frontier in plant mechanosensing?Biophys Rev. 2017 Aug;9(4):389-403. doi: 10.1007/s12551-017-0302-6. Epub 2017 Aug 12. Biophys Rev. 2017. PMID: 28801801 Free PMC article. Review.
-
"Laminopathies": a wide spectrum of human diseases.Exp Cell Res. 2007 Jun 10;313(10):2121-33. doi: 10.1016/j.yexcr.2007.03.028. Epub 2007 Mar 30. Exp Cell Res. 2007. PMID: 17467691 Free PMC article. Review.
Publication types
MeSH terms
Substances
Associated data
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials