Nuclear envelope remodelling during rat spermiogenesis: distribution and expression pattern of LAP2/thymopoietins

1998 ◽  
Vol 111 (15) ◽  
pp. 2227-2234 ◽  
Author(s):  
M. Alsheimer ◽  
E. Fecher ◽  
R. Benavente
Keyword(s):  
Nuclear Envelope ◽  
Single Gene ◽  
Nuclear Periphery ◽  
Nuclear Lamina ◽  
Integral Membrane Protein ◽  
Differentiation Process ◽  
Lamin B1 ◽  
The Third ◽  
Third Phase ◽  
The Family

Lamina-associated polypeptide 2 (LAP2) and the thymopoietins (TPs) are a family of proteins described in somatic cells of mammals, which are derived by alternative splicing from a single gene. For one of the members of the family (LAP2 = TPbeta) it has been shown that this integral membrane protein locates to the inner membrane of the nuclear envelope, and that it binds to chromatin and B-type lamins. In the present study, we observed that during the third phase of spermatogenesis (i.e. spermiogenesis), TP-labelling shifted progressively to one half of the nuclear periphery in round spermatids. In the elongating spermatid the signal then becomes restricted to one spot located at the posterior (centriolar) pole of the nucleus. Changes in localization are accompanied by the disappearance, first of TPgamma, and later on of LAP2/TPbeta. TPalpha is the only member of the family detectable in the mature sperm. Concomitantly, lamin B1, the only nuclear lamina protein known to be expressed in mammalian spermatids, showed a similar behaviour, i.e. shifted progressively to the centriolar pole of spermatid nuclei before it became undetectable in fully differentiated mature sperms. These results are the first demonstration that expression and localization patterns of TPs are coordinately and differentially regulated with lamins during a differentiation process.

scholarly journals Deformation of the nucleus by TGFβ1 via the remodeling of nuclear envelope and histone isoforms

2022 ◽  
Vol 15 (1) ◽  
Author(s):  
Ya-Hui Chi ◽  
Wan-Ping Wang ◽  
Ming-Chun Hung ◽  
Gunn-Guang Liou ◽  
Jing-Ya Wang ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Cell Lines ◽  
Nuclear Periphery ◽  
Nuclear Lamina ◽  
Lamin A ◽  
Nuclear Deformation ◽  
Smad Signaling ◽  
Lamin B1 ◽  
Compositional Changes ◽  
Nucleosomal Structure

AbstractThe cause of nuclear shape abnormalities which are often seen in pre-neoplastic and malignant tissues is not clear. In this study we report that deformation of the nucleus can be induced by TGFβ1 stimulation in several cell lines including Huh7. In our results, the upregulated histone H3.3 expression downstream of SMAD signaling contributed to TGFβ1-induced nuclear deformation, a process of which requires incorporation of the nuclear envelope (NE) proteins lamin B1 and SUN1. During this process, the NE constitutively ruptured and reformed. Contrast to lamin B1 which was relatively stationary around the nucleus, the upregulated lamin A was highly mobile, clustering at the nuclear periphery and reintegrating into the nucleoplasm. The chromatin regions that lost NE coverage formed a supra-nucleosomal structure characterized by elevated histone H3K27me3 and histone H1, the formation of which depended on the presence of lamin A. These results provide evidence that shape of the nucleus can be modulated through TGFβ1-induced compositional changes in the chromatin and nuclear lamina.

scholarly journals Deformation of the nucleus by TGFβ1 via the remodeling of nuclear envelope and histone isoforms

2021 ◽  
Author(s):  
Ya-Hui Chi ◽  
Wan-Ping Wang ◽  
Ming-Chun Hung ◽  
Gunn-Guang Liou ◽  
Jing-Ya Wang ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Dna Damage Response ◽  
Nuclear Periphery ◽  
Nuclear Lamina ◽  
Lamin A ◽  
Nuclear Deformation ◽  
Lamin B1 ◽  
Damage Response ◽  
Compositional Changes ◽  
Nucleosomal Structure

Abstract The cause of nuclear shape abnormalities which are often seen in pre-neoplastic and malignant tissues is not clear. In this study we report that deformation of the nucleus can be induced by TGFβ1 stimulation in several cell lines including Huh7. In our results, the upregulated histone H3.3 expression downstream of SMAD signaling contributed to TGFβ1-induced nuclear deformation, a process of which requires incorporation of the nuclear envelope (NE) proteins lamin B1 and SUN1. During this process, the NE constitutively ruptured and reformed with no observable indications of DNA damage response. Contrast to lamin B1 which was relatively stationary around the nucleus, the upregulated lamin A was highly mobile, shuttling between the nucleus and cytoplasm, and clustering at the nuclear periphery. The chromatin regions that lost NE coverage formed a supra-nucleosomal structure characterized by elevated histone H3K27me3 and histone H1, the formation of which depended on the presence of lamin A. These results provide evidence that shape of the nucleus can be modulated through TGFβ1-induced compositional changes in the chromatin and nuclear lamina.

scholarly journals Deformation of the nucleus by TGFβ1 via the remodeling of nuclear envelope and histone isoforms

2021 ◽  
Author(s):  
Ya-Hui Chi ◽  
Wan-Ping Wang ◽  
Ming-Chun Hung ◽  
Gunn-Guang Liou ◽  
Jing-Ya Wang ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Dna Damage Response ◽  
Nuclear Periphery ◽  
Nuclear Lamina ◽  
Lamin A ◽  
Nuclear Deformation ◽  
Lamin B1 ◽  
Damage Response ◽  
Compositional Changes ◽  
Nucleosomal Structure

Abstract The cause of nuclear shape abnormalities which are often seen in pre-neoplastic and malignant tissues is not clear. In this study we report that deformation of the nucleus can be induced by TGFb1 stimulation in several cell lines including Huh7. In our results, the upregulated histone H3.3 expression downstream of SMAD signaling contributed to TGFb1-induced nuclear deformation, a process of which requires incorporation of the nuclear envelope (NE) proteins lamin B1 and SUN1. During this process, the NE constitutively ruptured and reformed with no observable indications of DNA damage response. Contrast to lamin B1 which was relatively stationary around the nucleus, the upregulated lamin A was highly mobile, shuttling between the nucleus and cytoplasm, and clustering at the nuclear periphery. The chromatin regions that lost NE coverage formed a supra-nucleosomal structure characterized by elevated histone H3K27me3 and histone H1, the formation of which depended on the presence of lamin A. These results provide evidence that shape of the nucleus can be modulated through TGFb1-induced compositional changes in the chromatin and nuclear lamina.

scholarly journals Deformation of the Nucleus by TGFβ1 Via the Remodeling of Nuclear Envelope and Histone Isoforms

2021 ◽  
Author(s):  
Ya-Hui Chi ◽  
Wan-Ping Wang ◽  
Ming-Chun Hung ◽  
Gunn-Guang Liou ◽  
Jing-Ya Wang ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Dna Damage Response ◽  
Nuclear Periphery ◽  
Nuclear Lamina ◽  
Lamin A ◽  
Nuclear Deformation ◽  
Lamin B1 ◽  
Damage Response ◽  
Compositional Changes ◽  
Nucleosomal Structure

Abstract The cause of nuclear shape abnormalities which are often seen in pre-neoplastic and malignant tissues is not clear. In this study we report that deformation of the nucleus can be induced by TGFb1 stimulation in several cell lines including Huh7. In our results, the upregulated histone H3.3 expression downstream of SMAD signaling contributed to TGFb1-induced nuclear deformation, a process of which requires incorporation of the nuclear envelope (NE) proteins lamin B1 and SUN1. During this process, the NE constitutively ruptured and reformed with no observable indications of DNA damage response. Contrast to lamin B1 which was relatively stationary around the nucleus, the upregulated lamin A was highly mobile, shuttling between the nucleus and cytoplasm, and clustering at the nuclear periphery. The chromatin regions that lost NE coverage formed a supra-nucleosomal structure characterized by elevated histone H3K27me3 and histone H1, the formation of which depended on the presence of lamin A. These results provide evidence that shape of the nucleus can be modulated through TGFb1-induced compositional changes in the chromatin and nuclear lamina.

scholarly journals Lamin B1 acetylation slows the G1 to S cell cycle transition through inhibition of DNA repair

2021 ◽  
Author(s):  
Laura A Murray-Nerger ◽  
Joshua L Justice ◽  
Pranav Rekapalli ◽  
Josiah E Hutton ◽  
Ileana M Cristea
Keyword(s):  
Cell Cycle ◽  
Dna Repair ◽  
Posttranslational Modifications ◽  
Cell Cycle Progression ◽  
Nuclear Periphery ◽  
Virus Production ◽  
Nuclear Lamina ◽  
Regulatory Function ◽  
Herpesvirus Type ◽  
Lamin B1

Abstract The integrity and regulation of the nuclear lamina is essential for nuclear organization and chromatin stability, with its dysregulation being linked to laminopathy diseases and cancer. Although numerous posttranslational modifications have been identified on lamins, few have been ascribed a regulatory function. Here, we establish that lamin B1 (LMNB1) acetylation at K134 is a molecular toggle that controls nuclear periphery stability, cell cycle progression, and DNA repair. LMNB1 acetylation prevents lamina disruption during herpesvirus type 1 (HSV-1) infection, thereby inhibiting virus production. We also demonstrate the broad impact of this site on laminar processes in uninfected cells. LMNB1 acetylation negatively regulates canonical nonhomologous end joining by impairing the recruitment of 53BP1 to damaged DNA. This defect causes a delay in DNA damage resolution and a persistent activation of the G1/S checkpoint. Altogether, we reveal LMNB1 acetylation as a mechanism for controlling DNA repair pathway choice and stabilizing the nuclear periphery.

The 3D IFB SWOT Analysis as a Strategic Tool to Develop Entrepreneurial Plans for Family Businesses

2020 ◽  
pp. 363-389
Author(s):  
Luz Leyda Vega-Rosado
Keyword(s):  
Family Business ◽  
Swot Analysis ◽  
Three Dimensional ◽  
Family Firm ◽  
Second Phase ◽  
The Third ◽  
Third Phase ◽  
The Family ◽  
Generational Groups ◽  
The Individual

This chapter provides a framework that family business members can use to strategically and entrepreneurially evaluate themselves before they prepare the final strategic plan of the family firm. The tool consists of four phases. The first phase is the Strengths-Weaknesses-Opportunities-Threats (SWOT) analysis of the Individuals that are members of the family business. The second phase is the SWOT analysis of the Family's generational groups. Each generation in the family business will work in groups according to their year of birth. The third phase is the SWOT analysis of the Business. The fourth and most important phase is the integration called 3D IFB SWOT Analysis. It is 3D because it is three-dimensional, integrating the Individual, the Family's generations, and the Business.

scholarly journals A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation

2003 ◽  
Vol 162 (7) ◽  
pp. 1223-1232 ◽  
Author(s):  
Christopher P. Maske ◽  
Michael S. Hollinshead ◽  
Niall C. Higbee ◽  
Martin O. Bergo ◽  
Stephen G. Young ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Lamina ◽  
Potential Mechanism ◽  
Interphase Nuclei ◽  
Lamin B1 ◽  
Carboxyl Terminal ◽  
Caax Motif

The mammalian nuclear lamina protein lamin B1 is posttranslationally modified by farnesylation, endoproteolysis, and carboxymethylation at a carboxyl-terminal CAAX motif. In this work, we demonstrate that the CAAX endoprotease Rce1 is required for lamin B1 endoproteolysis, demonstrate an independent pool of proteolyzed but nonmethylated lamin B1, as well as fully processed lamin B1, in interphase nuclei, and show a role for methylation in the organization of lamin B1 into domains of the nuclear lamina. Deficiency in the endoproteolysis or methylation of lamin B1 results in loss of integrity and deformity of the nuclear lamina. These data show that the organization of the nuclear envelope and lamina is dependent on a mechanism involving the methylation of lamin B1, and they identify a potential mechanism of laminopathy involving a B-type lamin.

scholarly journals Chromosome length and gene density contribute to micronuclear membrane stability

2021 ◽  
Author(s):  
Anna Mammel ◽  
Heather Z Huang ◽  
Amanda L Gunn ◽  
Emma Choo ◽  
Emily M Hatch
Keyword(s):  
Nuclear Envelope ◽  
Membrane Integrity ◽  
Nuclear Lamina ◽  
Chromosome Length ◽  
Gene Density ◽  
Membrane Stability ◽  
Nuclear Pore ◽  
Membrane Rupture ◽  
Lamin B1 ◽  
Nuclear Envelope Assembly

Micronuclei are derived from missegregated chromosomes and frequently lose membrane integrity, leading to DNA damage, innate immune activation, and metastatic signaling. Here we demonstrate that two characteristics of the trapped chromosome, length and gene density, are key contributors to micronuclei membrane stability in human cells. Chromosome length is proportional to micronuclei size, and gene density has an additive effect with micronucleus size on membrane stability. We demonstrate that these results are not due to chromosome-specific differences in spindle position or initial nuclear pore complex recruitment during post-mitotic nuclear envelope assembly. We find that chromosome length and micronuclei size strongly correlate with lamin B1 and nuclear pore density in intact micronuclei. Unexpectedly, lamin B1 levels do not predict nuclear lamina organization and membrane stability. Instead, small gene-dense micronuclei have decreased nuclear lamina gaps compared to large micronuclei, despite very low levels of lamin B1. Our data strongly suggest that nuclear envelope composition defects previously correlated with membrane rupture only partly explain membrane stability in micronuclei. We propose that an unknown factor linked to gene density has a separate function that inhibits the appearance of nuclear lamina gaps and delays membrane rupture until late in the cell cycle.

scholarly journals Colocalization of intranuclear lamin foci with RNA splicing factors

1999 ◽  
Vol 112 (24) ◽  
pp. 4651-4661 ◽  
Author(s):  
G. Jagatheesan ◽  
S. Thanumalayan ◽  
B. Muralikrishna ◽  
N. Rangaraj ◽  
A.A. Karande ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Rna Splicing ◽  
Nuclear Periphery ◽  
Nuclear Lamina ◽  
Splicing Factors ◽  
Lamin A ◽  
Lamin B1 ◽  
Differential Reactivity ◽  
Fibrous Network

The lamins form a fibrous network underlying the inner nuclear membrane termed the nuclear lamina. In order to gain insights into the role of lamins in nuclear organization, we have characterized a monoclonal antibody (LA-2H10) raised against recombinant rat lamin A that labels nuclei in a speckled pattern in all cells of unsynchronized populations of HeLa and rat F-111 fibroblast cells, unlike the typical nuclear periphery staining by another monoclonal antibody to lamin A, LA-2B3. In immunolocalization studies the lamin A speckles or foci were found to colocalize with the RNA splicing factors SC-35 and U5-116 kD, but not with p80 coilin found in coiled bodies. Lamin B1 was also associated with these foci. These foci dispersed when cells entered mitosis and reformed during anaphase. The differential reactivity of LA-2H10 and LA-2B3 was retained after nuclei were extracted with detergents, nucleases and salt to disrupt interactions of lamins with chromatin and other nuclear proteins. Using deletion fragments of recombinant lamin A, the epitope recognized by LA-2H10 was located between amino acids 171 and 246. Our findings are consistent with a structural role for lamins in supporting nuclear compartments containing proteins involved in RNA splicing.

scholarly journals Chromosome length and gene density contribute to micronuclear membrane stability

2021 ◽  
Vol 5 (2) ◽  
pp. e202101210
Author(s):  
Anna E Mammel ◽  
Heather Z Huang ◽  
Amanda L Gunn ◽  
Emma Choo ◽  
Emily M Hatch
Keyword(s):  
Nuclear Envelope ◽  
Membrane Integrity ◽  
Nuclear Lamina ◽  
Chromosome Length ◽  
Gene Density ◽  
Membrane Stability ◽  
Nuclear Pore ◽  
Membrane Rupture ◽  
Lamin B1 ◽  
Nuclear Envelope Assembly

Micronuclei are derived from missegregated chromosomes and frequently lose membrane integrity, leading to DNA damage, innate immune activation, and metastatic signaling. Here, we demonstrate that two characteristics of the trapped chromosome, length and gene density, are key contributors to micronuclei membrane stability and determine the timing of micronucleus rupture. We demonstrate that these results are not due to chromosome-specific differences in spindle position or initial protein recruitment during post-mitotic nuclear envelope assembly. Micronucleus size strongly correlates with lamin B1 levels and nuclear pore density in intact micronuclei, but, unexpectedly, lamin B1 levels do not completely predict nuclear lamina organization or membrane stability. Instead, small gene-dense micronuclei have decreased nuclear lamina gaps compared to large micronuclei, despite very low levels of lamin B1. Our data strongly suggest that nuclear envelope composition defects previously correlated with membrane rupture only partly explain membrane stability in micronuclei. We propose that an unknown factor linked to gene density has a separate function that inhibits the appearance of nuclear lamina gaps and delays membrane rupture until late in the cell cycle.

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