Nuclear Lamins: Their Structure, Assembly, and Interactions

Stuurman, Nico; Heins, Susanne; Aebi, Ueli

doi:10.1006/jsbi.1998.3987

Cited by 673 publications

(584 citation statements)

References 176 publications

Supporting

Mentioning

556

Contrasting

Unclassified

Order By: Relevance

“…In pre-and postnatal nuclear matrices, the relative concentrations of lamin C were greater than lamin A, and in the adult nuclear matrix, the ratio of lamin A to lamin C changed in favour of lamin A (lane 10). The A-type lamins increase with terminal differentiation and growth arrest, suggesting a role for A-type lamins in cellular quiescence (20). In light of the recently reported decrease in transcriptional activity of the lamin A gene in adult rats (18), the increased concentration of lamin A could be the result of its slower turnover.…”

Section: Resultsmentioning

confidence: 99%

The Protein Composition of the Hepatocyte Nuclear Matrix Is Differentiation‐Stage Specific

Ivanović‐Matić¹,

Dinić²,

Vujošević³

et al. 2000

IUBMB Life

View full text Add to dashboard Cite

SummaryThe protein composition of hepatocyte nuclear matrices was examined in rats from the 16th day of gestation to 75 days after birth (adult). An overall increase in size of the nuclear matrix was accompanied by quantitative and qualitative changes in its protein content. Quantitative changes of the major proteins of the peripheral lamina surrounding the isolated nuclear matrix were detected. By Western analysis we established that in pre-and postnatal nuclear matrices the relative concentrations of lamin C were greater than lamin A. After birth, the relative concentrations of both lamins progressively increased. In the adult nuclear matrix, the concentration of lamin A was greater than lamin C. In contrast, the relative concentrations of lamin B remained unchanged throughout development and growth. The relative concentrations of two nuclear matrix -associated regulatory proteins studied changed with development and growth: transcription factor C/EBP® isoforms, which were detected during the gestation period, increased notably after the rst postnatal day, attaining a maximum at the adult stage; the high concentrations of the proliferating cell nuclear antigen (PCNA) perceptibly decreased after the 21st prenatal day. Changes in the composition of the nuclear matrix protein suggest that this structure coordinates nuclear functioning during cell differentiation.IUBMB Life, 49: 511 -517, 2000 Keywords C/EBPa ; hepatocyte development; lamins; nuclear matrix; PCNA.The nuclear matrix is a proteinaceous structural framework of the nucleus. The isolated matrix has a tripartite structure and

show abstract

Section: Resultsmentioning

confidence: 99%

The Protein Composition of the Hepatocyte Nuclear Matrix Is Differentiation‐Stage Specific

Ivanović‐Matić¹,

Dinić²,

Vujošević³

et al. 2000

IUBMB Life

View full text Add to dashboard Cite

show abstract

mentioning

confidence: 99%

“…The nuclear lamina provides structural support for the nuclear membrane and attachment sites for chromatin. It is also required for a variety of essential cellular functions, including nuclear assembly following mitosis, DNA replication, and transcription (11,29).The nuclear lamina is composed primarily of type V intermediate filament proteins known as lamins. Lamin structure is conserved in multicellular eukaryotes, and individual lamin filaments consist of multiple coiled-coil dimers linked in a head-to-tail fashion.…”

mentioning

confidence: 99%

Conformational Changes in the Nuclear Lamina Induced by Herpes Simplex Virus Type 1 Require Genes U _L 31 and U _L 34

Reynolds

Liang

Baines

2004

J Virol

159

209

View full text Add to dashboard Cite

The herpes simplex virus type 1 (HSV-1) U L 31 and U L 34 proteins are dependent on each other for proper targeting to the nuclear membrane and are required for efficient envelopment of nucleocapsids at the inner nuclear membrane. In this work, we show that whereas the solubility of lamins A and C (lamin A/C) was not markedly increased, HSV induced conformational changes in the nuclear lamina of infected cells, as viewed after staining with three different lamin A/C-specific antibodies. In one case, reactivity with a monoclonal antibody that recognizes an epitope in the lamin tail domain was greatly reduced in HSV-infected cells. This apparent HSV-induced epitope masking required both U L 31 and U L 34, but these proteins were not sufficient to mask the epitope in uninfected cells, indicating that other HSV proteins are also required. In the second case, staining with a rabbit polyclonal antibody that primarily recognizes epitopes in the lamin A/C rod domain revealed that U L 34 is required for HSV-induced decreased availability of epitopes for reaction with the antibody, whereas U L 31 protein was dispensable for this effect. Still another polyclonal antibody indicated virtually no difference in lamin A/C staining in infected versus uninfected cells, indicating that the HSVinduced changes are more conformational than the result of lamin depletion at the nuclear rim. Further evidence supporting an interaction between the nuclear lamina and the U L 31/U L 34 protein complex includes the observations that (i) overexpression of the U L 31 protein in uninfected cells was sufficient to relocalize lamin A/C from the nuclear rim into nucleoplasmic aggregates, (ii) overexpression of U L 34 was sufficient to relocalize some lamin A/C into the cytoplasm, and (iii) both U L 31 and U L 34 could directly bind lamin A/C in vitro. These studies suggest that the U L 31 and U L 34 proteins modify the conformation of the nuclear lamina in infected cells, possibly by direct interaction with lamin A/C, and that other proteins are also likely involved. Given that the nuclear lamina potentially excludes nucleocapsids from envelopment sites at the inner nuclear membrane, the lamina alteration may reflect a role of the U L 31/U L 34 protein complex in perturbing the lamina to promote nucleocapsid egress from the nucleus. Alternatively, the data are compatible with a role of the lamina in targeting the U L 31/U L 34 protein complex to the nuclear membrane.The nuclear envelope consists of two leaflets, defined as the inner nuclear membrane and outer nuclear membrane. The perinuclear space, defined as the space between the two leaflets, is continuous with the lumen of the endoplasmic reticulum. A network of predominantly insoluble cellular proteins, the nuclear lamina, lines the nucleoplasmic face of the inner nuclear membrane. The nuclear lamina provides structural support for the nuclear membrane and attachment sites for chromatin. It is also required for a variety of essential cellular functions, including nuclear assembly following mi...

show abstract

“…Lamins are intermediate filament proteins and are major components of the nuclear lamina playing an important role in cell regulation and structural integrity [14][15][16][17] . There are well over 100 mutations in the LMNA gene, encoding for the protein lamin A/C, that result in more than 10 clinical disorders collectively referred to as laminopathies [37,43] .…”

Section: Discussionmentioning

confidence: 99%

“…LMNA consists of 12 exons and at exon 10 alternative splicing occurs giving rise to the proteins lamin A (664 amino acids) and lamin C (572 amino acids). The first 566 amino acids (exon 1-10) of lamin A and C (lamin A/C) are identical which code for an amino terminal globular head domain, central rod domain (coil 1a, 1b, and 2), and a portion of the carboxyl terminal globular tail domain [17,26] . Mutations in the human LMNA gene encoding for lamin A/C results in several different clinical disorders referred to as "laminopathies" [27][28][29][30][31][32][33][34][35] .…”

Section: Introductionmentioning

confidence: 99%

Beyond membrane channelopathies: alternative mechanisms underlying complex human disease

Boudoulas

Mohler

2011

Acta Pharmacol Sin

View full text Add to dashboard Cite

Nuclear Lamins: Their Structure, Assembly, and Interactions

Cited by 673 publications

References 176 publications

The Protein Composition of the Hepatocyte Nuclear Matrix Is Differentiation‐Stage Specific

The Protein Composition of the Hepatocyte Nuclear Matrix Is Differentiation‐Stage Specific

Conformational Changes in the Nuclear Lamina Induced by Herpes Simplex Virus Type 1 Require Genes U _L 31 and U _L 34

Beyond membrane channelopathies: alternative mechanisms underlying complex human disease

Contact Info

Product

Resources

About

Nuclear Lamins: Their Structure, Assembly, and Interactions

Cited by 673 publications

References 176 publications

The Protein Composition of the Hepatocyte Nuclear Matrix Is Differentiation‐Stage Specific

The Protein Composition of the Hepatocyte Nuclear Matrix Is Differentiation‐Stage Specific

Conformational Changes in the Nuclear Lamina Induced by Herpes Simplex Virus Type 1 Require Genes U L 31 and U L 34

Beyond membrane channelopathies: alternative mechanisms underlying complex human disease

Contact Info

Product

Resources

About

Conformational Changes in the Nuclear Lamina Induced by Herpes Simplex Virus Type 1 Require Genes U _L 31 and U _L 34