Nuclear lamins: laminopathies and their role in premature ageing.

@article{Broers2006NuclearLL,
  title={Nuclear lamins: laminopathies and their role in premature ageing.},
  author={Jos L V Broers and Frans C. S. Ramaekers and Gisèle Bonne and Rabah Ben Yaou and Christopher J. Hutchison},
  journal={Physiological reviews},
  year={2006},
  volume={86 3},
  pages={
          967-1008
        }
}
It has been demonstrated that nuclear lamins are important proteins in maintaining cellular as well as nuclear integrity, and in maintaining chromatin organization in the nucleus. Moreover, there is growing evidence that lamins play a prominent role in transcriptional control. The family of laminopathies is a fast-growing group of diseases caused by abnormalities in the structure or processing of the lamin A/C (LMNA) gene. Mutations or incorrect processing cause more than a dozen different… 
A-type lamins preserve genomic stability
TLDR
Recent studies reveal novel functions for A-type lamins in the maintenance of telomeres and in the DNA damage response (DDR) path way, which shed some light onto the putative molecular mechanisms by which alterations in A- type lamins induce genomic instability and contrib ute to disease.
A-type lamin networks in light of laminopathic diseases.
Nurturing the genome
TLDR
Recent studies revealing novel functions for A- type lamins in the maintenance of telomeres and in the DNA damage response (DDR) pathway have shed some light on the molecular mechanisms by which alterations in A-type lamins induce genomic instability and contribute to disease.
Nurturing the genome: A-type lamins preserve genomic stability.
TLDR
Recent studies revealing novel functions for A-type lamins in the maintenance of telomeres and in the DNA damage response (DDR) pathway are discussed to shed some light onto the putative molecular mechanisms by which alterations in A- type lamins induce genomic instability and contribute to disease.
Laminopathies: un seul gène, de nombreuses pathologies.
TLDR
The exploration of pathophysiological mechanisms of LMNA mutations largely benefits from the numerous mouse models created, which have been widely used to analyze affected molecular pathways and to test putative therapeutic treatments.
Nuclear Lamins and Neurobiology
TLDR
This review summarizes recent progress in elucidating links between nuclear lamins and neurobiology and uncovers a peculiar pattern of nuclear lamin expression in the brain.
Mapping of lamin A- and progerin-interacting genome regions
TLDR
It is demonstrated that progerin induces global changes in chromatin organization by enhancing interactions with a specific subset of genes in addition to the identified lamin A-associated genes, and provides novel insights into the role of lamin–chromatin interactions in Chromatin organization.
Nuclear Lamins in the Brain — New Insights into Function and Regulation
TLDR
It is intriguing that the adult brain preferentially expresses lamin C rather than lamin A, very likely due to microRNA-mediated removal of prelamin A transcripts, which is thought to participate in many important functions within the cell nucleus.
The nuclear envelope proteins Kugelkern and Narf and their putative role in aging
TLDR
It is demonstrated that Narf is involved in aging-related processes as loss-of function experiments decreased Drosophila`s lifespan whereas constitutively higher expression by multiple genomic copies or UAS overexpression led to a prolongation in lifespan.
Causes and consequences of genomic instability in laminopathies: Replication stress and interferon response
TLDR
Recent studies showing that lamins play a role in DNA replication are summarized, and the emerging model that DNA damage and replication stress are “sensed” at the cytoplasm by proteins that normally survey this space in search of foreign nucleic acids is discussed.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 441 REFERENCES
Lamins in disease: why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes?
TLDR
An examination of how lamins A/C, emerin and other integral membrane proteins interact at the INM provides the basis for a novel model for how mutations that promote disease phenotypes are likely to influence these interactions and therefore cause cellular pathology through a combination of weakness of the lamina or altered gene expression.
Nuclear envelope proteins and associated diseases
TLDR
A group of markedly heterogeneous disorders can be classified as ‘nuclear envelopathies’ because of the presence of specific abnormalities of the nuclear envelope.
Lamin B1 is required for mouse development and nuclear integrity.
TLDR
These mutant mice and cell lines derived from them will be useful models for studying the role of the nuclear lamina in various cellular processes and provide evidence for a broad and nonredundant function of lamin B1 in mammalian development.
Formation of nuclear splicing factor compartments is independent of lamins A/C.
TLDR
It is shown that the morphology and cellular properties of splicing factor compartments are independent of A- and C-type lamins, and an essential structural role of lamins A/C inSplicing factor compartment morphology is argued against.
Nuclear envelope alterations in fibroblasts from patients with muscular dystrophy, cardiomyopathy, and partial lipodystrophy carrying lamin A/C gene mutations
TLDR
Results confirm that mutations in lamins A and C may lead to a weakening of a structural support network in the nuclear envelope in fibroblasts and that nuclear architecture changes depend upon the location of the mutation in different domains of lamin A/C.
Defects in nuclear structure and function promote dilated cardiomyopathy in lamin A/C-deficient mice.
TLDR
It is suggested that lamin A/C-deficient mice develop rapidly progressive dilated cardiomyopathy (DCM), a model in which the primary pathophysiological mechanism in Lmna(-/-) mice is defective force transmission resulting from disruption of lamin interactions with the muscle-specific desmin network and loss of cytoskeletal tension.
Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy.
TLDR
Results suggest that nuclear structural defects could contribute to the etiology of both dilated cardiomyopathy and autosomal dominant Emery-Dreifuss muscular dystrophy.
Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson–Gilford progeria syndrome
TLDR
It is shown by light and electron microscopy that HGPS is associated with significant changes in nuclear shape, including lobulation of the nuclear envelope, thickening of thenuclear lamina, loss of peripheral heterochromatin, and clustering of nuclear pores.
The Nuclear Envelope in Muscular Dystrophy and Cardiovascular Diseases
TLDR
Observations clearly demonstrate that A‐type lamins in particular play a central role, not only in the maintenance of nuclear envelope integrity but also in the large‐scale organization of nuclear architecture.
Loss of a-Type Lamin Expression Compromises Nuclear Envelope Integrity Leading to Muscular Dystrophy
TLDR
It is shown that mice lacking A-type lamins develop to term with no overt abnormalities, however, their postnatal growth is severely retarded and is characterized by the appearance of muscular dystrophy.
...
1
2
3
4
5
...