Changes in Nucleoporin Domain Topology in Response to Chemical Effectors

Paulillo, Sara M.; Powers, Maureen A.; Ullman, Katharine S.; Fahrenkrog, Birthe

doi:10.1016/j.jmb.2006.08.021

Cited by 38 publications

(39 citation statements)

References 49 publications

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“…of the nucleoplasmic basket structure could be distinguished underpinning the role of Ca 2+ in structural rearrangements of the NPC. [28][29][30][31] Intriguingly, Bax and Bak, initially characterized as key players in apoptotic cytochrome C release from mitochondria, were later involved in maintaining ER [Ca 2+ ]. Cells lacking both Bax and Bak were shown to have a drastically reduced ER [Ca 2+ ] and fail to mobilize Ca 2+ from the ER to mitochondria.…”

Section: Introductionmentioning

confidence: 99%

Regulation of nuclear envelope permeability in cell death and survival

Straßer

Grote²,

Schäuble³

et al. 2012

Nucleus

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Section: Introductionmentioning

confidence: 99%

Regulation of nuclear envelope permeability in cell death and survival

Straßer

Grote²,

Schäuble³

et al. 2012

Nucleus

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“…Nup153's FG-domain was detected all over the nuclear basket and occasionally on the cytoplasmic side of the NPC, suggesting a high mobility of this domain (Nakielny et al, 1999;Fahrenkrog et al, 2002;Paulillo et al, 2005;Paulillo et al, 2006;Lim et al, 2007) (Fig. 3B).…”

Section: The Nucleoporin Nup153: Domain Organization and Localizationmentioning

confidence: 97%

The nuclear pore complex: structure and function

Duhéron¹,

Fahrenkrog²

2017

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Forkhead box P3 (FOXP3), a gene member of the forkhead/winged-helix family of transcription regulators, is Nuclear pore complexes (NPCs) are large multi-protein complexes, which are embedded in the nuclear envelope and which are regulating the molecular exchange between the nucleus and the cytoplasm. While electron microscopy and cryo-electron tomography studies have provided high-resolution pictures of the NPC structure as entity, the challenge nowadays is to elucidate the organization and the functions of nuclear pore proteins (nucleoporins or Nups) inside and outside the NPC. Nucleoporins are not only involved in nucleocytoplasmic transport, but in an increasing number of other cellular processes, such as kinetochore organization, cell cycle regulation, DNA repair, and gene expression. The implication of nucleoporins in these diverse processes links them also to a wide variety of human diseases, such as cancer and autoimmune diseases. Here we review the progress made in defining the molecular arrangement of nucleoporins within the NPC and use the example of Nup153 to illustrate the versatility of individual nucleoporins and their implication in various human diseases.

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“…As reported, this NPC-mediated transport of various large molecules (such as DNAs, RNAs) is related to the Ca 2+ pump. 56 In some mammalian cell nuclei, extracellular ATP activates purinergic receptors such as P2Y2 and P2X4, which induces an increase in the free Ca 2+ concentration in the cell nuclei. To balance the Ca 2+ transient, cADP-ribose and the intracellular messenger, inositol 1,4,5-triphosphate [Ins(1,4,5)P 3 , IP 3 ], can trigger the release of partial nuclear Ca 2+ through the actions of inositol 1,4,5-trisphosphate receptors (IP 3 R), indicating a role for extracellular ATP in regulating nuclear function, by increasing nuclear Ca 2+ concentrations.…”

Section: Extracellular Atp Increases Viability Of Cells Treated With mentioning

confidence: 99%

“…To balance the Ca 2+ transient, cADP-ribose and the intracellular messenger, inositol 1,4,5-triphosphate [Ins(1,4,5)P 3 , IP 3 ], can trigger the release of partial nuclear Ca 2+ through the actions of inositol 1,4,5-trisphosphate receptors (IP 3 R), indicating a role for extracellular ATP in regulating nuclear function, by increasing nuclear Ca 2+ concentrations. 47,[56][57][58][59][60] Since inositol is metabolically linked to IP 3 within mammalian cells, [42][43][44][45][46] this course may consume INO ligands in the PG6-PEI-INO vectors and result in unpacking of vector/pDNA complexes, and further inhibit transgene expression. Relevant mechanisms were predicted and shown in Figure 10.…”

Section: Extracellular Atp Increases Viability Of Cells Treated With mentioning

confidence: 99%

Using inositol as a biocompatible ligand for efficient transgene expression

Zhang¹,

Bellis²,

Fan³

et al. 2015

IJN

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Transgene transfection techniques using cationic polymers such as polyethylenimines (PEIs) and PEI derivatives as gene vectors have shown efficacy, although they also have shortcomings. PEIs have decent DNA-binding capability and good cell internalization performance, but they cannot deliver gene payloads very efficiently to cell nuclei. In this study, three hyperbranched polyglycerol-polyethylenimine (PG6-PEI) polymers conjugated with myo-inositol (INO) molecules were developed. The three resulting PG6-PEI-INO polymers have an increased number of INO ligands per molecule. PG6-PEI-INO 1 had only 14 carboxymethyl INO (CMINO) units per molecule. PG6-PEI-INO 2 had approximately 130 CMINO units per molecule. PG6-PEI-INO 3 had as high as 415 CMINO units approximately. Mixing PG6-PEI-INO polymers with DNA produced compact nanocomposites. We then performed localization studies using fluorescent microscopy. As the number of conjugated inositol ligands increased in PG6-PEI-INO polymers, there was a corresponding increase in accumulation of the polymers within 293T cell nuclei. Transfection performed with spherical 293T cells yielded 82% of EGFP-positive cells when using PG6-PEI-INO 3 as the vehicle. Studies further revealed that extracellular adenosine triphosphate (eATP) can inhibit the transgene efficiency of PG6-PEI-INO polymers, as compared with PEI and PG6-PEI that were not conjugated with inositol. Our work unveiled the possibility of using inositol as an effective ligand for transgene expression.

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Changes in Nucleoporin Domain Topology in Response to Chemical Effectors

Cited by 38 publications

References 49 publications

Regulation of nuclear envelope permeability in cell death and survival

Regulation of nuclear envelope permeability in cell death and survival

The nuclear pore complex: structure and function

Using inositol as a biocompatible ligand for efficient transgene expression

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Changes in Nucleoporin Domain Topology in Response to Chemical Effectors

Cited by 38 publications

References 49 publications

Regulation of nuclear envelope permeability in cell death and survival

Regulation of nuclear envelope permeability in cell death and survival

The nuclear pore complex: structure and function

Using inositol as a biocompatible ligand for&nbsp;efficient transgene expression

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Using inositol as a biocompatible ligand for efficient transgene expression