Spatial chromatin organization and gene regulation at the nuclear lamina

Guerreiro, Isabel; Kind, Jop

doi:10.1016/j.gde.2019.04.008

Cited by 47 publications

(35 citation statements)

References 66 publications

(83 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Lamins form helical dimers that interact with each other in a head-to-tail orientation assembling into a protein meshwork. Current models of nuclear organization suggest that nuclear lamina is important for the maintenance and functioning of the 3D chromosome architecture by interacting with both the nuclear membrane and chromatin [4][5][6][7][8]. However, the precise players and mechanisms of these interactions are unknown.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Reorganization of the nuclear architecture in the Drosophila melanogaster Lamin B mutant lacking the CaaX box

Bondarenko

Sharakhov

2020

Nucleus

View full text Add to dashboard Cite

Lamins interact with the nuclear membrane and chromatin but the precise players and mechanisms of these interactions are unknown. Here, we tested whether the removal of the CaaX motif from Lamin B disrupts its attachment to the nuclear membrane and affects chromatin distribution. We used Drosophila melanogaster Lam A25 homozygous mutants that lack the CaaX box. We found that the mutant Lamin B was not confined to the nuclear periphery but was distributed throughout the nuclear interior, colocalizing with chromosomes in salivary gland and proventriculus. The peripheral position of Lamin C, nuclear pore complex (NPC), heterochromatin protein 1a (HP1a), H3K9me2-and H3K27me3associated chromatin remained intact. The fluorescence intensity of the DAPI-stained peripheral chromatin significantly decreased and that of the central chromatin significantly increased in the proventriculus nuclei of the mutantflies compared to wild-type. However, the mutation had little effect on chromatin radial distribution inside highly polytenized salivary gland nuclei.

show abstract

Section: Introductionmentioning

confidence: 99%

“…The C-terminal tail domain, including the CaaX box, may also be responsible for this function [ 15 , 17 ]. In addition, the CaaX motif plays a crucial role in the process of lamina filament assembly providing head-to-tail interaction between linearly ordered lamin dimers in the eventual composition of the in vivo polymer [ 5 ].…”

Section: Introductionmentioning

confidence: 99%

Reorganization of the nuclear architecture in the Drosophila melanogaster Lamin B mutant lacking the CaaX box

Bondarenko

Sharakhov

2020

Nucleus

View full text Add to dashboard Cite

show abstract

“…The unique proteome of the inner nuclear membrane is ensured by nuclear pore complexes that restrict diffusion between the peripheral ER and the nucleoplasm (Schirmer et al, 2003). The inner nuclear membrane proteins, including lamins, give the nucleus its unique shape and are crucial for chromosome organization, and DNA replication and repair (Guerreiro and Kind, 2019). Interestingly, RCE1 and ZMPSTE24 are important for the removal of the last three amino acids from the so-called CAAX proteins (where 'C' is a prenylated cysteine that is important for membrane attachment, 'A' is an aliphatic amino acid and 'X' is any amino acid) (see poster).…”

Section: Endoplasmic Reticulum and Inner Nuclear Membranementioning

confidence: 99%

Intramembrane proteolysis at a glance: from signalling to protein degradation

Kühnle

Dederer

Lemberg

2019

Journal of Cell Science

View full text Add to dashboard Cite

Over the last two decades, a group of unusual proteases, so-called intramembrane proteases, have become increasingly recognized for their unique ability to cleave peptide bonds within cellular membranes. They are found in all kingdoms of life and fulfil versatile functions ranging from protein maturation, to activation of signalling molecules, to protein degradation. In this Cell Science at a Glance article and the accompanying poster, we focus on intramembrane proteases in mammalian cells. By comparing intramembrane proteases in different cellular organelles, we set out to review their functions within the context of the roles of individual cellular compartments. Additionally, we exemplify their mode of action in relation to known substrates by distinguishing cleavage events that promote degradation of substrate from those that release active domains from the membrane bilayer.

show abstract

“…While the importance of lamins in control of gene expression is becoming more and more evident (for a recent review, see, e.g., in [ 36 ]), this review will focus on another important aspect of lamins function, i.e., their role in structural support, mechanosensing, and mechanoresponse of cells. Their role in healthy cells is described below.…”

Section: Introductionmentioning

confidence: 99%

Structural and Mechanical Aberrations of the Nuclear Lamina in Disease

Stiekema

Zandvoort

Ramaekers

et al. 2020

Cells

View full text Add to dashboard Cite

The nuclear lamins are the major components of the nuclear lamina in the nuclear envelope. Lamins are involved in numerous functions, including a role in providing structural support to the cell and the mechanosensing of the cell. Mutations in the genes encoding for lamins lead to the rare diseases termed laminopathies. However, not only laminopathies show alterations in the nuclear lamina. Deregulation of lamin expression is reported in multiple cancers and several viral infections lead to a disrupted nuclear lamina. The structural and mechanical effects of alterations in the nuclear lamina can partly explain the phenotypes seen in disease, such as muscular weakness in certain laminopathies and transmigration of cancer cells. However, a lot of answers to questions about the relation between changes in the nuclear lamina and disease development remain elusive. Here, we review the current understandings of the contribution of the nuclear lamina in the structural support and mechanosensing of healthy and diseased cells.

show abstract

Spatial chromatin organization and gene regulation at the nuclear lamina

Cited by 47 publications

References 66 publications

Reorganization of the nuclear architecture in the Drosophila melanogaster Lamin B mutant lacking the CaaX box

Reorganization of the nuclear architecture in the Drosophila melanogaster Lamin B mutant lacking the CaaX box

Intramembrane proteolysis at a glance: from signalling to protein degradation

Structural and Mechanical Aberrations of the Nuclear Lamina in Disease

Contact Info

Product

Resources

About