Identification and Cloning of an mRNA Coding for a Germ Cell-Specific A-Type Lamin in Mice

Inagaki, Hidehito; Hotta, Yasuo

doi:10.1006/excr.1994.1164

Cited by 179 publications

(138 citation statements)

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“…Lamin A and C, alternatively spliced products of the LMNA locus, are the predominant A-type lamins. A third member of the A-type lamin family, lamin C2, is restricted in expression to germ cells (17). Indeed, the lamin A͞C binding protein, LAP2␣, interacts with pRB and is important for nuclear tethering of the tumor suppressor (18).…”

mentioning

confidence: 99%

A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation

Johnson

Nitta²,

Frock³

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

255

249

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The retinoblastoma protein (pRB) is a critical regulator of cell proliferation and differentiation and an important tumor suppressor. In the G1 phase of the cell cycle, pRB localizes to perinucleolar sites associated with lamin A͞C intranuclear foci. Here, we examine pRB function in cells lacking lamin A͞C, finding that pRB levels are dramatically decreased and that the remaining pRB is mislocalized. We demonstrate that A-type lamins protect pRB from proteasomal degradation. Both pRB levels and localization are restored upon reintroduction of lamin A. Lmna ؊/؊ cells resemble Rb ؊/؊ cells, exhibiting altered cell-cycle properties and reduced capacity to undergo cell-cycle arrest in response to DNA damage. These findings establish a functional link between a core nuclear structural component and an important cell-cycle regulator. They further raise the possibility that altered pRB function may be a contributing factor in dystrophic syndromes arising from LMNA mutation.

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mentioning

confidence: 99%

A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation

Johnson

Nitta²,

Frock³

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

255

249

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“…LMNA encodes A‐type lamins produced by alternative splicing of its pre‐mRNA. The two major isoforms of this A‐type include lamin A and lamin C, but minor isoforms have also been described: lamin AΔ10, lamin C2 (Furukawa, Inagaki & Hotta, 1994; Lin & Worman, 1993; Machiels et al., 1996), and more recently LMNAΔ447 and LMNAΔ297 (DeBoy et al., 2017). Lamins A and C are mainly expressed in the nucleus of differentiated somatic cells.…”

Section: Lamins and Laminopathiesmentioning

confidence: 99%

“…Lamins A and C are mainly expressed in the nucleus of differentiated somatic cells. Concerning B‐type lamins, LMNB1 encodes lamin B1, whereas LMNB2 encodes lamins B2 and B3 by alternative splicing (Elkhatib et al., 2015; Furukawa et al., 1994; Feng Lin & Worman, 1995). Lamins B1 and B2 are expressed in nearly all somatic cells, while lamin B3 is a specific spermatid type.…”

Section: Lamins and Laminopathiesmentioning

confidence: 99%

MicroRNAs in hereditary and sporadic premature aging syndromes and other laminopathies

et al. 2018

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SummaryHereditary and sporadic laminopathies are caused by mutations in genes encoding lamins, their partners, or the metalloprotease ZMPSTE24/FACE1. Depending on the clinical phenotype, they are classified as tissue‐specific or systemic diseases. The latter mostly manifest with several accelerated aging features, as in Hutchinson–Gilford progeria syndrome (HGPS) and other progeroid syndromes. MicroRNAs are small noncoding RNAs described as powerful regulators of gene expression, mainly by degrading target mRNAs or by inhibiting their translation. In recent years, the role of these small RNAs has become an object of study in laminopathies using in vitro or in vivo murine models as well as cells/tissues of patients. To date, few miRNAs have been reported to exert protective effects in laminopathies, including miR‐9, which prevents progerin accumulation in HGPS neurons. The recent literature has described the potential implication of several other miRNAs in the pathophysiology of laminopathies, mostly by exerting deleterious effects. This review provides an overview of the current knowledge of the functional relevance and molecular insights of miRNAs in laminopathies. Furthermore, we discuss how these discoveries could help to better understand these diseases at the molecular level and could pave the way toward identifying new potential therapeutic targets and strategies based on miRNA modulation.

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“…Interestingly, certain cases of laminopathies primarily affect the heart resulting in dilated cardiomyopathy with or without conduction system disease even though lamin is found in all differentiated cells in the human body [27][28][29] . LMNA also encodes the protein lamin C2 found in germ cells that is encoded by an alternative first exon [36] .…”

Section: Introductionmentioning

confidence: 99%

Beyond membrane channelopathies: alternative mechanisms underlying complex human disease

Boudoulas

Mohler

2011

Acta Pharmacol Sin

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Identification and Cloning of an mRNA Coding for a Germ Cell-Specific A-Type Lamin in Mice

Cited by 179 publications

References 0 publications

A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation

A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation

MicroRNAs in hereditary and sporadic premature aging syndromes and other laminopathies

Beyond membrane channelopathies: alternative mechanisms underlying complex human disease

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