Lamins: the structure and protein complexes

Gruenbaum, Yosef; Medalia, Ohad

doi:10.1016/j.ceb.2014.09.009

Cited by 93 publications

(89 citation statements)

References 43 publications

(45 reference statements)

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“…Although some association of nuclear lamins is observed during early stages of NE reformation 103 the bulk of nuclear lamins are reassembled into the lamina only after the nuclei have regained competence for nuclear import 26; 222 . Arrangements of lamins into the lamina during interphase has been studied intensively, but we still miss a clear picture of how the assembly process occurs (reviewed in 223 ). Similarly, we do not know when the interactions to NPCs are established 103; 224 occurring most likely via the lamin-interacting nucleoporin Nup153 225; 226 .…”

Section: Lamina and Linc Complex Reassemblymentioning

confidence: 95%

Nuclear Reformation at the End of Mitosis

Schellhaus

Magistris

Antonin

2016

Journal of Molecular Biology

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Section: Lamina and Linc Complex Reassemblymentioning

confidence: 95%

Nuclear Reformation at the End of Mitosis

Schellhaus

Magistris

Antonin

2016

Journal of Molecular Biology

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“…Among the various laminopathies, which are hereditary diseases resulting from mutations in genes encoding the nuclear lamina or lamina-associated proteins [42], myelination is impacted only in adult-onset autosomal dominant leukodystrophy (ADLD). This disease characterized by myelin loss in adults and represents a defect in myelin maintenance that is caused by duplication of LMNB1 [20,21].…”

Section: Introductionmentioning

confidence: 99%

Epigenetic control of oligodendrocyte development: adding new players to old keepers

Liu

Moyon

Hernandez

et al. 2016

Current Opinion in Neurobiology

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Emerging and strengthening evidence suggests an important role of myelin in plasticity and axonal survival. However, the mechanisms regulating progression from oligodendrocyte progenitor cells (OPCs) to myelinating oligodendrocytes remain only partially understood. A series of overlapping yet distinct epigenetic events occur as a proliferating OPC exits the cell cycle, initiates differentiation, and becomes a myelin-forming oligodendrocyte that wraps axons. Here we discuss recent advances towards understanding the epigenetic control of oligodendrocyte development that integrates environmental stimuli. We suggest that OPCs are directly responsive to extrinsic signals due to predominantly euchromatic nuclei, while the heterochromatic nuclei render differentiating and myelinating cells less susceptible to signals modulating the epigenome.

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“…One of the most conserved characteristics of genome organization is the accumulation of heterochromatin close to the nuclear lamina, which comprises a meshwork of four lamin proteins and a number of transmembrane proteins in mammals (reviewed in Amendola and van Steensel, 2014;Gruenbaum and Medalia, 2015). Three genes LMNA, LMNB1 and LMNB2 encode the four major mammalian lamins: the splice variants lamin A and C, lamin B1 and lamin B2.…”

Section: Introductionmentioning

confidence: 99%

MacroH2A histone variants maintain nuclear organization and heterochromatin architecture

Douet

Corujo

Malinverni

et al. 2017

Journal of Cell Science

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Genetic loss-of-function studies on development, cancer and somatic cell reprogramming have suggested that the group of macroH2A histone variants might function through stabilizing the differentiated state by a yet unknown mechanism. Here, we present results demonstrating that macroH2A variants have a major function in maintaining nuclear organization and heterochromatin architecture. Specifically, we find that a substantial amount of macroH2A is associated with heterochromatic repeat sequences. We further identify macroH2A on sites of interstitial heterochromatin decorated by histone H3 trimethylated on K9 (H3K9me3). Loss of macroH2A leads to major defects in nuclear organization, including reduced nuclear circularity, disruption of nucleoli and a global loss of dense heterochromatin. Domains formed by DNA repeat sequences are disorganized, expanded and fragmented, and mildly re-expressed when depleted of macroH2A. At the molecular level, we find that macroH2A is required for the interaction of repeat sequences with the nucleostructural protein lamin B1. Taken together, our results argue that a major function of macroH2A histone variants is to link nucleosome composition to higher-order chromatin architecture.

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Lamins: the structure and protein complexes

Cited by 93 publications

References 43 publications

Nuclear Reformation at the End of Mitosis

Nuclear Reformation at the End of Mitosis

Epigenetic control of oligodendrocyte development: adding new players to old keepers

MacroH2A histone variants maintain nuclear organization and heterochromatin architecture

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