Abstract
Lamins are major components of the nuclear lamina, a network of proteins that supports the nuclear envelope in metazoan cells. Over the past decade, biochemical studies have provided support for the view that lamins are not passive bystanders providing mechanical stability to the nucleus but play an active role in the organization of the genome and the function of fundamental nuclear processes. It has also become apparent that lamins are critical for human health, as a large number of mutations identified in the gene that encodes for A-type lamins are associated with tissue-specific and systemic genetic diseases, including the accelerated aging disorder known as Hutchinson-Gilford progeria syndrome. Recent years have witnessed great advances in our understanding of the role of lamins in the nucleus and the functional consequences of disease-associated A-type lamin mutations. Many of these findings have been presented in comprehensive reviews. In this mini-review, we discuss recent breakthroughs in the role of lamins in health and disease and what lies ahead in lamin research.
Highlights
Lamins are major components of the nuclear lamina, a network of proteins that supports the nuclear envelope in metazoan cells
A-type lamin A and C are encoded by the LMNA gene and generated by alternative splicing, whereas B-type lamin B1 and B2 are encoded by two separate genes: LMNB1 and LMNB2
Determining the function of lamins is of critical importance for human health because of the large number of mutations identified across the LMNA gene that are associated with a class of human disorders, collectively known as laminopathies, whose clinical symptoms include skeletal or cardiac muscular dystrophy, lipodystrophy, dysplasia, dermopathy, neuropathy, leukodystrophy, and accelerated aging[9,10]
Summary
Eriksson M, Brown WT, Gordon LB, et al.: Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Gonzalo S, Kreienkamp R: DNA repair defects and genome instability in Hutchinson-Gilford Progeria Syndrome. Swift J, Ivanovska IL, Buxboim A, et al.: Nuclear lamin-A scales with tissue stiffness and enhances matrix-directed differentiation. Ihalainen TO, Aires L, Herzog FA, et al.: Differential basal-to-apical accessibility of lamin A/C epitopes in the nuclear lamina regulated by changes in cytoskeletal tension. Zwerger M, Jaalouk DE, Lombardi ML, et al.: Myopathic lamin mutations impair nuclear stability in cells and tissue and disrupt nucleo-cytoskeletal coupling.
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