Lamin B2 is a protein that in humans is encoded by the LMNB2 gene. It is the second of two type B nuclear lamins, and it is associated with laminopathies. The LMNB2 gene also codes for the testis-specific transcript, Lamin B3 generated by alternative splicing.[5] Relative to its other isoforms, lamin B2 is the least abundant lamin in the nuclei of somatic cells.[6] Like all lamins, its structure is composed of an α-helical central rod domain with a N-terminal globular head domain and a C-terminal tail.[6]
Function
Lamin B2 along with its isoforms comprise the nuclear matrix that is responsible for maintaining nucleus shape and the organization of chromatin. B2 has been shown to form mesh-like structures with other lamins along the nuclear envelope.[6] These meshworks associate with LINC complexes, inner nuclear membrane proteins and underlying chromatin.[6][7][8] In addition to its localization along the nuclear envelope, B2 also plays a role in regulating nucleolar morphology. It associates with nucleolin and nucleophosmin and localizes to the granular component of nucleoli. It has been shown to regulate expression of the 45S rRNA.[9]
Neurodevelopment
Lamin B2 is also a necessary factor in nuclear translocation, an important step in neuronal migration during embryonic development of the cerebral cortex. However, the role of B2 in the process has not yet been characterized as it is not an interactor of the LINC complex.[5][10]
See also
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000176619 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000062075 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b Coffinier C, Chang SY, Nobumori C, Tu Y, Farber EA, Toth JI, et al. (March 2010). "Abnormal development of the cerebral cortex and cerebellum in the setting of lamin B2 deficiency". Proceedings of the National Academy of Sciences of the United States of America. 107 (11): 5076–5081. doi:10.1073/pnas.0908790107. PMC 2841930. PMID 20145110.
- ^ a b c d Shimi T, Kittisopikul M, Tran J, Goldman AE, Adam SA, Zheng Y, et al. (November 2015). "Structural organization of nuclear lamins A, C, B1, and B2 revealed by superresolution microscopy". Molecular Biology of the Cell. 26 (22): 4075–4086. doi:10.1091/mbc.E15-07-0461. PMC 4710238. PMID 26310440.
- ^ Meinke P, Schirmer EC (September 2015). "LINC'ing form and function at the nuclear envelope". FEBS Letters. 589 (19 Pt A): 2514–2521. doi:10.1016/j.febslet.2015.06.011. PMID 26096784.
- ^ Brachner A, Foisner R (2014), "Lamina-Associated Polypeptide (LAP)2α and Other LEM Proteins in Cancer Biology", in Schirmer EC, de las Heras JI (eds.), Cancer Biology and the Nuclear Envelope: Recent Advances May Elucidate Past Paradoxes, Advances in Experimental Medicine and Biology, vol. 773, New York, NY: Springer, pp. 143–163, doi:10.1007/978-1-4899-8032-8_7, ISBN 978-1-4899-8032-8, PMC 4333762, PMID 24563347
- ^ Sen Gupta A, Sengupta K (December 2017). "Lamin B2 Modulates Nucleolar Morphology, Dynamics, and Function". Molecular and Cellular Biology. 37 (24) e00274-17: e00274–17. doi:10.1128/MCB.00274-17. PMC 5705821. PMID 28993479.
- ^ Coffinier C, Fong LG, Young SG (2010). "LINCing lamin B2 to neuronal migration: growing evidence for cell-specific roles of B-type lamins". Nucleus. 1 (5): 407–411. doi:10.4161/nucl.1.5.12830. PMC 3027074. PMID 21278813.
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See also: cytoskeletal defects |