The Nuclear Life of Nucleoporins

Kalverda, Bernike; Fornerod, Maarten

doi:10.1016/j.devcel.2007.07.008

Cited by 13 publications

(13 citation statements)

References 10 publications

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“…By viewing signals from two perspectives, it is possible to distinguish co-localized and disparate immunolabeling. Nucleoporin immunofluorescent signals emanating from the nuclear envelope (contralateral surfaces and rim) are likely to represent NPCs, whereas intranuclear signals, by definition, would not arise from NPCs and may represent nucleoporins involved in functions other than nucleocytoplasmic transport [40].…”

Section: Resultsmentioning

confidence: 99%

Nuclear Distributions of NUP62 and NUP214 Suggest Architectural Diversity and Spatial Patterning among Nuclear Pore Complexes

et al. 2012

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The shape of nuclei in many adherent cultured cells approximates an oblate ellipsoid, with contralateral flattened surfaces facing the culture plate or the medium. Observations of cultured cell nuclei from orthogonal perspectives revealed that nucleoporin p62 (NUP62) and nucleoporin 214 (NUP214) are differentially distributed between nuclear pore complexes on the flattened surfaces and peripheral rim of the nucleus. High resolution stimulated emission depletion (STED) immunofluorescence microscopy resolved individual NPCs, and suggested both heterogeneity and microheterogeneity in NUP62 and NUP214 immunolabeling among in NPC populations. Similar to nuclear domains and interphase chromosome territories, architectural diversity and spatial patterning of NPCs may be an intrinsic property of the nucleus that is linked to the functions and organization of underlying chromatin.

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Section: Resultsmentioning

confidence: 99%

Nuclear Distributions of NUP62 and NUP214 Suggest Architectural Diversity and Spatial Patterning among Nuclear Pore Complexes

et al. 2012

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“…These studies on nucleoporin dynamics are consistent with the very slow protein turnover of scaffold nucleoporins (D’Angelo et al, 2009; Daigle et al, 2001). The scaffold structure of the NPC can be viewed as a docking site for more mobile nucleoporins, which often have functional roles at sites away from the NPC (Kalverda and Fornerod, 2007). …”

Section: Dynamicsmentioning

confidence: 99%

The Nuclear Pore Complex Has Entered the Atomic Age

et al. 2009

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Nuclear pore complexes (NPCs) perforate the nuclear envelope and represent the exclusive passageway into and out of the nucleus of the eukaryotic cell. Apart from their essential transport function, components of the NPC have important, direct roles in nuclear organization and in gene regulation. Due to its central role in cell biology, it is of considerable interest to determine the NPC structure at atomic resolution. The complexity of these large, 40-60 MDa protein assemblies has for decades limited such structural studies. More recently, exploiting the intrinsic modularity of the NPC, structural biologists are making progress toward understanding this nanomachine in molecular detail. Structures of building blocks of the stable, architectural scaffold of the NPC have been solved, and distinct models for their assembly proposed. Here we review the status of the field and lay out the challenges and the next steps toward a full understanding of the NPC at atomic resolution.

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“…In this context, epigenetic hallmarks are key players of nucleoporin-chromatin interaction, but the molecular mechanisms by which this happens remain obscure, although there is evidence that chromatin remodeling factors such as CREB binding protein, HDAC1, SAGA and TREX-2 interact with nucleoporins, especially the ones with FG repeats. [56][57][58][59][60][61] We have not been able to identify the molecular mechanisms by means of which the 3 studied nucleoporins form the reported INCs. However, HDAC inhibitors could be an experimental model to study epigenetic hallmarks mediating interactions between nucleoporins and chromatin.…”

Section: Discussionmentioning

confidence: 99%

Nucleoporins redistribute inside the nucleus after cell cycle arrest induced by histone deacetylases inhibition

Pérez-Garrastachu

Arluzea

Andrade

et al. 2017

Nucleus

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(2017) Nucleoporins redistribute inside the nucleus after cell cycle arrest induced by histone deacetylases inhibition, Nucleus, 8:5, 515-533, DOI: 10.1080/19491034.2017 To link to this article: https://doi.org/10. 1080/19491034.2017 ABSTRACTNucleoporins are the main components of the nuclear-pore complex (NPC) and were initially considered as mere structural elements embedded in the nuclear envelope, being responsible for nucleocytoplasmic transport. Nevertheless, several recent scientific reports have revealed that some nucleoporins participate in nuclear processes such as transcription, replication, DNA repair and chromosome segregation. Thus, the interaction of NPCs with chromatin could modulate the distribution of chromosome territories relying on the epigenetic state of DNA. In particular, the nuclear basket proteins Tpr and Nup153, and the FG-nucleoporin Nup98 seem to play key roles in all these novel functions. In this work, histone deacetylase inhibitors (HDACi) were used to induce a hyperacetylated state of chromatin and the behavior of the mentioned nucleoporins was studied. Our results show that, after HDACi treatment, Tpr, Nup153 and Nup98 are translocated from the nuclear pore toward the interior of the cell nucleus, accumulating as intranuclear nucleoporin clusters. These transitory structures are highly dynamic, and are mainly present in the population of cells arrested at the G0/G1 phase of the cell cycle. Our results indicate that the redistribution of these nucleoporins from the nuclear envelope to the nuclear interior may be implicated in the early events of cell cycle initialization, particularly during the G1 phase transition.

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The Nuclear Life of Nucleoporins

Cited by 13 publications

References 10 publications

Nuclear Distributions of NUP62 and NUP214 Suggest Architectural Diversity and Spatial Patterning among Nuclear Pore Complexes

Nuclear Distributions of NUP62 and NUP214 Suggest Architectural Diversity and Spatial Patterning among Nuclear Pore Complexes

The Nuclear Pore Complex Has Entered the Atomic Age

Nucleoporins redistribute inside the nucleus after cell cycle arrest induced by histone deacetylases inhibition

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