Nuclear size, nuclear pore number and cell cycle

Maeshima, Kazuhiro; Iino, Haruki; Hihara, Saera; Imamoto, Naoko

doi:10.4161/nucl.2.2.15446

Cited by 42 publications

(37 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…During normal interphase, nuclear volume and NPC number nearly double, however distinct mechanisms seem to regulate these two processes because disruption of interphase NPC assembly in HeLa cells by cyclin-dependent kinase inhibition negligibly affected nuclear growth [23,24]. Nonetheless, altered NPC composition can affect nuclear size.…”

Section: Introductionmentioning

confidence: 99%

Sizing and shaping the nucleus: mechanisms and significance

Jevtić

Edens

Vuković

et al. 2014

Current Opinion in Cell Biology

154

130

View full text Add to dashboard Cite

The size and shape of the nucleus are tightly regulated, indicating the physiological significance of proper nuclear morphology, yet the mechanisms and functions of nuclear size and shape regulation remain poorly understood. Correlations between altered nuclear morphology and certain disease states have long been observed, most notably many cancers are diagnosed and staged based on graded increases in nuclear size. Here we review recent studies investigating the mechanisms regulating nuclear size and shape, how mitotic events influence nuclear morphology, and the role of nuclear size and shape in subnuclear chromatin organization and cancer progression.

show abstract

Section: Introductionmentioning

confidence: 99%

Sizing and shaping the nucleus: mechanisms and significance

Jevtić

Edens

Vuković

et al. 2014

Current Opinion in Cell Biology

154

130

View full text Add to dashboard Cite

show abstract

“…10 Furthermore, NPC assembly and nuclear expansion are independently regulated in mammalian tissue culture cells, as blocking interphasic NPC assembly in HeLa cells did not alter nuclear expansion or size. 16,17 On the other hand, mutations that cause NPC clustering and/or mislocalization frequently give rise to altered nuclear morphology. [18][19][20][21] Taken together, NPC composition seems to contribute more to the regulation of nuclear size than NPC number or density.…”

Section: Nucleocytoplasmic Transport and Nuclear Morphologymentioning

confidence: 99%

Recent advances in understanding nuclear size and shape

Mukherjee

Chen

Levy

2016

Nucleus

View full text Add to dashboard Cite

Size and shape are important aspects of nuclear structure. While normal cells maintain nuclear size within a defined range, altered nuclear size and shape are associated with a variety of diseases. It is unknown if altered nuclear morphology contributes to pathology, and answering this question requires a better understanding of the mechanisms that control nuclear size and shape. In this review, we discuss recent advances in our understanding of the mechanisms that regulate nuclear morphology, focusing on nucleocytoplasmic transport, nuclear lamins, the endoplasmic reticulum, the cell cycle, and potential links between nuclear size and size regulation of other organelles. We then discuss the functional significance of nuclear morphology in the context of early embryonic development. Looking toward the future, we review new experimental approaches that promise to provide new insights into mechanisms of nuclear size control, in particular microfluidic-based technologies, and discuss how altered nuclear morphology might impact chromatin organization and physiology of diseased cells.

show abstract

“…NPCs mediate selective trafficking of proteins and other macromolecules between the nucleus and the cytoplasm but also serve other important functions, including gene activation and mRNA surveillance (5,6). The biogenesis of NPCs and their distribution over the NE are highly regulated processes and are coordinated with the cell cycle (7). During interphase, the number of NPCs doubles.…”

mentioning

confidence: 99%

Yeast Integral Membrane Proteins Apq12, Brl1, and Brr6 Form a Complex Important for Regulation of Membrane Homeostasis and Nuclear Pore Complex Biogenesis

et al. 2015

View full text Add to dashboard Cite

bProper functioning of intracellular membranes is critical for many cellular processes. A key feature of membranes is their ability to adapt to changes in environmental conditions by adjusting their composition so as to maintain constant biophysical properties, including fluidity and flexibility. Similar changes in the biophysical properties of membranes likely occur when intracellular processes, such as vesicle formation and fusion, require dramatic changes in membrane curvature. Similar modifications must also be made when nuclear pore complexes (NPCs) are constructed within the existing nuclear membrane, as occurs during interphase in all eukaryotes. Here we report on the role of the essential nuclear envelope/endoplasmic reticulum (NE/ER) protein Brl1 in regulating the membrane composition of the NE/ER. We show that Brl1 and two other proteins characterized previously-Brr6, which is closely related to Brl1, and Apq12-function together and are required for lipid homeostasis. All three transmembrane proteins are localized to the NE and can be coprecipitated. As has been shown for mutations affecting Brr6 and Apq12, mutations in Brl1 lead to defects in lipid metabolism, increased sensitivity to drugs that inhibit enzymes involved in lipid synthesis, and strong genetic interactions with mutations affecting lipid metabolism. Mutations affecting Brl1 or Brr6 or the absence of Apq12 leads to hyperfluid membranes, because mutant cells are hypersensitive to agents that increase membrane fluidity. We suggest that the defects in nuclear pore complex biogenesis and mRNA export seen in these mutants are consequences of defects in maintaining the biophysical properties of the NE. T he nuclear envelope (NE) of eukaryotic cells compartmentalizes the nuclear material and separates it from the cytoplasm. The double membrane of the NE consists of an outer and an inner nuclear membrane (ONM and INM) that differ in protein and lipid composition. The NE is structurally and functionally related to the endoplasmic reticulum (ER), and the ONM is contiguous with the ER (1, 2). Embedded in the NE are the nuclear pore complexes (NPCs) and, in budding yeast, the spindle pole body (SPB). NPCs are extremely large and are constructed from multiple copies of about 30 different nucleoporins (nups) (3, 4). NPCs mediate selective trafficking of proteins and other macromolecules between the nucleus and the cytoplasm but also serve other important functions, including gene activation and mRNA surveillance (5, 6). The biogenesis of NPCs and their distribution over the NE are highly regulated processes and are coordinated with the cell cycle (7). During interphase, the number of NPCs doubles. In budding yeast, the NE remains intact throughout the cell cycle, and all the formation of NPCs occurs through de novo construction within the NE.In addition to the ONM and the INM, the NE contains a pore membrane domain (POM), formed by the fusion of the INM and ONM at sites where NPCs are assembled (8). The POM is a highly curved region of the NE that is i...

show abstract

Nuclear size, nuclear pore number and cell cycle

Cited by 42 publications

References 37 publications

Sizing and shaping the nucleus: mechanisms and significance

Sizing and shaping the nucleus: mechanisms and significance

Recent advances in understanding nuclear size and shape

Yeast Integral Membrane Proteins Apq12, Brl1, and Brr6 Form a Complex Important for Regulation of Membrane Homeostasis and Nuclear Pore Complex Biogenesis

Contact Info

Product

Resources

About