The Nuclear Lamina as an Organizer of Chromosome Architecture

Shevelyov, Yuri Y.; Ulianov, Sergey V.

doi:10.3390/cells8020136

Cited by 86 publications

(80 citation statements)

References 102 publications

(201 reference statements)

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“…There is considerable interest in understanding how the heterochromatin compartment is organized at the nuclear envelope, and how lineage-inappropriate genes are silenced through such positioning (Amendola and van Steensel, 2014;Buchwalter et al, 2019;Gordon et al, 2015;Gruenbaum and Foisner, 2015;Harr et al, 2016;Lemaitre and Bickmore, 2015;Meister and Taddei, 2013;Padeken and Heun, 2014;Poleshko et al, 2017;Politz et al, 2013;Shevelyov and Nurminsky, 2012;Shevelyov and Ulianov, 2019;Ungricht and Kutay, 2015;van Steensel and Belmont, 2017;Wong and Reddy, 2015;Yanez-Cuna and van Steensel, 2017;Zullo et al, 2012). Emerging research findings have pointed to an evolutionarily conserved mechanism whereby a class of three "tethering proteins" function to organize H3K9me-modified heterochromatin at the nuclear periphery (Gonzalez-Sandoval et al, 2015;Harr et al, 2016;Kind et al, 2013;Poleshko et al, 2013;Towbin et al, 2013;van Steensel and Belmont, 2017).…”

Section: Discussionmentioning

confidence: 99%

“…A common element of this class of tethers is that H3K9me heterochromatin modifications serve as anchoring points for attachment of heterochromatin to the nuclear periphery. Two members of this class, LBR (Olins et al, 2010) and CEC-4 (Gonzalez-Sandoval et al, 2015;Harr et al, 2016;Shevelyov and Ulianov, 2019) anchor heterochromatin to nuclear membranes, and their roles in heterochromatin organization, as well as cell differentiation have been described (Gonzalez-Sandoval et al, 2015;Solovei et al, 2013).…”

Section: Discussionmentioning

confidence: 99%

“…The nuclear lamina is composed of the intermediate filament proteins Lamin A/C, Lamin B1 and Lamin B2. In addition to acting as a nuclear framework, the nuclear lamina serves as a docking site for heterochromatin, which forms a characteristic silent "peripheral heterochromatin compartment" decorated with the repressive heterochromatic histone tail modifications, histone 3 lysine 9 di-and tri-methyl (H3K9me2 and H3K9me3) (Buchwalter et al, 2019;Gordon et al, 2015;Gruenbaum and Foisner, 2015;Lemaitre and Bickmore, 2015;Meister and Taddei, 2013;Padeken and Heun, 2014;Politz et al, 2013;Shevelyov and Nurminsky, 2012;Shevelyov and Ulianov, 2019;van Steensel and Belmont, 2017;Wong and Reddy, 2015). This heterochromatin compartment positioned at the nuclear lamina is the focus of much interest, as it provides a critical function in housing lineage-inappropriate repressed genes and gene-poor DNA (Becker et al, 2016;Peric-Hupkes et al, 2010;Reddy et al, 2008;Stancheva and Schirmer, 2014;Zhou et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

“…LBR and PRR14 tethering proteins are now both characterized as associating strongly with the nuclear periphery, and binding to and constraining adjacent heterochromatin (Shevelyov and Ulianov, 2019). The tethering mechanism implicates a simple bivalent attachment mechanism, through the HP1 adapter molecule.…”

Section: Introductionmentioning

confidence: 99%

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The PRR14 heterochromatin tether encodes modular domains that mediate and regulate nuclear lamina targeting

Dunlevy

Medvedeva

Wilson

et al. 2019

Preprint

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AbstractA large fraction of epigenetically silent heterochromatin is anchored to the nuclear periphery via “tethering proteins” that function to bridge heterochromatin and the nuclear membrane or nuclear lamina. We identified previously a human tethering protein, PRR14, that binds heterochromatin through an N-terminal domain, but the mechanism and regulation of nuclear lamina association remained to be investigated. Here we identify a centrally located, evolutionarily conserved PRR14 nuclear lamina binding domain (LBD) that is both necessary and sufficient for positioning of PRR14 at the nuclear lamina. We also show that PRR14 associates dynamically with the nuclear lamina, and provide evidence that such dynamics are regulated through phosphorylation of the LBD. We also show that the evolutionary conserved PRR14 C-terminal Tantalus domain encodes a PP2A phosphatase recognition site that regulates PRR14 nuclear lamina association. The overall findings demonstrate a heterochromatin anchoring mechanism whereby the PRR14 tether simultaneously binds heterochromatin and the nuclear lamina through two modular domains. Furthermore, the identification of a modular LBD may provide an engineering strategy for delivery of cargo to the nuclear lamina.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The PRR14 heterochromatin tether encodes modular domains that mediate and regulate nuclear lamina targeting

Dunlevy

Medvedeva

Wilson

et al. 2019

Preprint

View full text Add to dashboard Cite

show abstract

“…Actively transcribed regions are spatially associated with nuclear pores or localized in the nuclear interior . Such spatial organization is considerably supported by the nuclear lamina, suggesting a significant role for the lamina in genome organization . Lamins are direct targets of CDKs , an interaction which results in their disassembly and solubilization during nuclear envelope breakdown at mitosis .…”

Section: Challenges Associated With Copying the Complex Epigenomementioning

confidence: 99%

Cell cycle dynamics in the reprogramming of cellular identity

Eastman

Guo

2019

FEBS Letters

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Reprogramming of cellular identity is fundamentally at odds with replication of the genome: cell fate reprogramming requires complex multidimensional epigenomic changes, whereas genome replication demands fidelity. In this review, we discuss how the pace of the genome's replication and cell cycle influences the way daughter cells take on their identity. We highlight several biochemical processes that are pertinent to cell fate control, whose propagation into the daughter cells should be governed by more complex mechanisms than simple templated replication. With this mindset, we summarize multiple scenarios where rapid cell cycle could interfere with cell fate copying and promote cell fate reprogramming. Prominent examples of cell fate regulation by specific cell cycle phases are also discussed. Overall, there is much to be learned regarding the relationship between cell fate reprogramming and cell cycle control. Harnessing cell cycle dynamics could greatly facilitate the derivation of desired cell types.

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Male triploid oysters of Crassostrea gigas exhibit defects in mitosis and meiosis during early spermatogenesis

et al. 2022

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The Pacific oyster, Crassostrea gigas is a successive irregular hermaphrodite mollusc which has an annual breeding cycle. Oysters are naturally diploid organisms, but triploid oysters have been developed for use in shellfish aquaculture, with the aim of obtaining sterile animals with commercial value. However, studies have shown that some triploid oysters are partially able to undergo gametogenesis, with numerous proliferating cells closed to diploids (3n alpha) or a partial one with an accumulation of locked germ cells (3n beta). The aim of our study therefore was to understand the regulation of spermatogenesis in both groups of triploid oysters (alpha and beta) from the beginning of spermatogenesis, during mitosis and meiosis events. Our results demonstrate that the reduced spermatogenesis in triploids results from a deregulation of the development of the germinal lineage and the establishment of the gonadal tract led by a lower number of tubules. Morphological cellular investigation also revealed an abnormal condensation of germ cell nuclei and the presence of clear patches in the nucleoplasm of triploid cells, which were more pronounced in beta oysters. Furthermore, studies of molecular and cellular regulation showed a downregulation of mitotic spindle checkpoint in beta oysters, resulting in disturbance of chromosomal segregation, notably on Spindle Assembly Checkpoint involved in the binding of microtubules to chromosomes. Taken together, our results suggest that the lower reproductive ability of triploid oysters may be due to cellular and molecular events such as impairment of spermatogenesis and disruptions of mitosis and meiosis, occurring early and at various stages of the gametogenetic cycle.

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The Nuclear Lamina as an Organizer of Chromosome Architecture

Cited by 86 publications

References 102 publications

The PRR14 heterochromatin tether encodes modular domains that mediate and regulate nuclear lamina targeting

The PRR14 heterochromatin tether encodes modular domains that mediate and regulate nuclear lamina targeting

Cell cycle dynamics in the reprogramming of cellular identity

Male triploid oysters of Crassostrea gigas exhibit defects in mitosis and meiosis during early spermatogenesis

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