An alternative hypothesis for the deformation of a cell nucleus

Scilight ◽  
2022 ◽  
Vol 2022 (1) ◽  
pp. 011106
Author(s):  
Avery Thompson
2006 ◽  
Vol 84 (3-4) ◽  
pp. 287-297 ◽  
Author(s):  
Fernand Gobeil ◽  
Audrey Fortier ◽  
Tang Zhu ◽  
Michela Bossolasco ◽  
Martin Leduc ◽  
...  

G-protein-coupled receptors (GPCRs) comprise a wide family of monomeric heptahelical glycoproteins that recognize a broad array of extracellular mediators including cationic amines, lipids, peptides, proteins, and sensory agents. Thus far, much attention has been given towards the comprehension of intracellular signaling mechanisms activated by cell membrane GPCRs, which convert extracellular hormonal stimuli into acute, non-genomic (e.g., hormone secretion, muscle contraction, and cell metabolism) and delayed, genomic biological responses (e.g., cell division, proliferation, and apoptosis). However, with respect to the latter response, there is compelling evidence for a novel intracrine mode of genomic regulation by GPCRs that implies either the endocytosis and nuclear translocation of peripheral-liganded GPCR and (or) the activation of nuclearly located GPCR by endogenously produced, nonsecreted ligands. A noteworthy example of the last scenario is given by heptahelical receptors that are activated by bioactive lipoids (e.g., PGE2 and PAF), many of which may be formed from bilayer membranes including those of the nucleus. The experimental evidence for the nuclear localization and signalling of GPCRs will be reviewed. We will also discuss possible molecular mechanisms responsible for the atypical compartmentalization of GPCRs at the cell nucleus, along with their role in gene expression.


Nature ◽  
1962 ◽  
Vol 195 (4840) ◽  
pp. 462-464 ◽  
Author(s):  
WERNER R. LOEWENSTEIN ◽  
YOSHINOBU KANNO

2006 ◽  
Vol 84 (3-4) ◽  
pp. 367-376 ◽  
Author(s):  
Christiane Rollenhagen ◽  
Nelly Panté

Uridine-rich small nuclear ribonucleoproteins (U snRNPs) are the building units of the spliceosome. These RNA and protein complexes assemble in the cytoplasm. After proper assembly and RNA maturation, mature U snRNPs are imported into the cell nucleus, where they take part in the splicing process. In this paper we review the current knowledge of how U snRNPs enter the nucleus.


PROTOPLASMA ◽  
2015 ◽  
Vol 253 (3) ◽  
pp. 943-956 ◽  
Author(s):  
Magda Dubińska-Magiera ◽  
Magdalena Chmielewska ◽  
Katarzyna Kozioł ◽  
Magdalena Machowska ◽  
Christopher J. Hutchison ◽  
...  

Abstract Xenopus LAP2β protein is the single isoform expressed in XTC cells. The protein localizes on heterochromatin clusters both at the nuclear envelope and inside a cell nucleus. The majority of XLAP2β fraction neither colocalizes with TPX2 protein during interphase nor can be immunoprecipitated with XLAP2β antibody. Knockdown of the XLAP2β protein expression in XTC cells by synthetic siRNA and plasmid encoded siRNA resulted in nuclear abnormalities including changes in shape of nuclei, abnormal chromatin structure, loss of nuclear envelope, mislocalization of integral membrane proteins of INM such as lamin B2, mislocalization of nucleoporins, and cell death. Based on timing of cell death, we suggest mechanism associated with nucleus reassembly or with entry into mitosis. This confirms that Xenopus LAP2 protein is essential for the maintenance of cell nucleus integrity and the process of its reassembly after mitosis.


2021 ◽  
Author(s):  
Amir Vahabikashi ◽  
Suganya Sivagurunathan ◽  
Fiona Ann Sadsad Nicdao ◽  
Yu Long Han ◽  
Chan Young Park ◽  
...  

The ability of a cell to regulate its mechanical properties is central to its function. Emerging evidence suggests that interactions between the cell nucleus and cytoskeleton influence cell mechanics through poorly understood mechanisms. Here we show that A- and B-type nuclear lamin isoforms distinctively modulate both nuclear and cellular volume and selectively stabilize the linker of nucleoskeleton and cytoskeleton (LINC) complexes that couple the nucleus to cytoskeletal actin and vimentin. We reveal, further, that loss of each of the four-known lamin isoforms in the mouse embryonic fibroblasts differentially affects cortical and cytoplasmic stiffness as well as cellular contractility, and then propose a LINC complex mediated model that explains these impaired mechanical phenotypes. Finally, we demonstrate that loss of each lamin isoform softens the nucleus in a manner that correlates with loss of heterochromatin. Together, these findings uncover distinctive roles for each lamin isoform in maintaining cellular and nuclear mechanics.


1946 ◽  
Vol 30 (2) ◽  
pp. 117-148 ◽  
Author(s):  
A. E. Mirsky ◽  
A. W. Pollister

A desoxyribose nucleoprotein complex, which we have referred to as a chromosin, has been prepared from a great variety of cells, mainly animal but also plant and bacterial. A chromosin is derived from the cell nucleus. In the course of preparation precautions have been taken to prevent contamination by cytoplasmic constituents. To assure the nuclear origin of all components of chromosin, nuclei have in several instances been isolated before extraction was begun. Because of the precautions taken, chromosins do not contain detectable quantities of ribose nucleoproteins; but, incidentally, extraction of ribose nucleoproteins, free of desoxyribose compounds, has also been described in this paper. A typical chromosin contains 3 components: desoxyribose nucleic acid, histone, and non-histone protein. The nucleic acid, being highly polymerized, is exceedingly viscous when dissolved and fibrous when precipitated. Histone and non-histone protein differ from each other in a number of ways, of which one of the most definite is that whereas a histone contains no more than traces of tryptophane, the non-histone protein of chromosin contains nearly 1 per cent of tryptophane. In neutral physiological saline both proteins can combine with nucleic acid. With the isolation of chromosins from so many different kinds of cells, it can now be seen that (contrary to the view expressed by Kossel) histones are present in most animal cells and at least in some plant and bacterial cells. Chromosin prepared from the Type III pneumococcus is active in transforming the type of a pneumococcus culture. It has been pointed out that it is not yet known whether or not protein is a necessary constituent of the transforming agent. To extract chromosin from a cell M NaCl is used. When dissolved in M NaCl the nucleic acid and histone components of a chromosin are to a considerable extent dissociated. They are not dissociated when the chromosin is dissolved in 0.02 M NaCl, but in this medium a partial depolymerization of the nucleic acid occurs. A chromosin should certainly not be considered to be a definite chemical compound. It is a complex extracted from chromatin, which is itself a complicated nuclear structure. And in the course of extraction, it need hardly be said, the structure of chromatin has been considerably changed. To avoid complications it has been considered an advantage in this work to begin with isolated nuclei, and it would clearly be a further simplification to begin chemical procedures only after the chromosomes themselves have been isolated. This is now being accomplished, and it is found that the methods described in this paper are of value in learning how the substances present in a chromosin are put together in a chromosome.


Sign in / Sign up

Export Citation Format

Share Document