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Cells
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Nucleocytoplasmic Transport
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Nucleocytoplasmic Transport

A special issue of Cells (ISSN 2073-4409).

Deadline for manuscript submissions: closed (20 June 2015) | Viewed by 68340

Special Issue Editor

Prof. Dr. Birthe Fahrenkrog

E-Mail Website
Guest Editor
Laboratoire du Biologie du Noyau, Institut de Biologie & de Médecine Moléculaire, Université Libre de Bruxelles, Rue Profs Jeener & Brachet, 12, B-6041 Charleroi, Belgium
Interests: nuclear pore complex; nucleocytoplasmic transport; nuclear envelope; lamins; apoptosis in yeast
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Nucleocytoplasmic transport is a critical cellular process and vitally important for normal cell function. Trafficking between the cytoplasm and the nucleus occurs through nuclear pore complexes, macromolecular assemblies that punctuate the nuclear envelope, and constituted of proteins, known as nucleoporins. We have made exceptional progress in our understanding of nucleocytoplasmic transport, nuclear pore complex architecture, and nucleoporin function in recent years and unravelled the plurality of cellular processes that are interconnected with the nucleocytoplasmic transport machinery. This Special Issue offers an Open Access forum at bringing together a collection of original research and review articles addressing the expanding aspects of nucleocytoplasmic transport and nuclear pore function. To that end, we are welcoming contributions that may cover molecular mechanisms or functions of nuclear pore proteins and nuclear transport factors, not only in nucleocytoplasmic transport and nuclear pore structure, but, also, for example, in the regulation of gene expression and the cell cycle, the crosstalk with other cell signalling programs, and the implication in health and disease. We hope to provide a stimulating collection that will further research in this fascinating field.

Prof. Dr. Birthe Fahrenkrog
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cells is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


Keywords

  • nucleocytoplasmic transport
  • karyopherin
  • Ran GTPase
  • nuclear pore complex
  • nucleoporin
  • nuclear pore complex assembly and disassembly
  • nuclear envelope
  • nuclear organization
  • gene expression
  • cell cycle
  • signalling
  • human disease

Published Papers (7 papers)

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Research

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3717 KiB  
Article
Active Nuclear Import of Membrane Proteins Revisited
by Justyna K. Laba, Anton Steen, Petra Popken, Alina Chernova, Bert Poolman and Liesbeth M. Veenhoff
Cells 2015, 4(4), 653-673; https://doi.org/10.3390/cells4040653 - 13 Oct 2015
Cited by 9 | Viewed by 6846
Abstract
It is poorly understood how membrane proteins destined for the inner nuclear membrane pass the crowded environment of the Nuclear Pore Complex (NPC). For the Saccharomyces cerevisiae proteins Src1/Heh1 and Heh2, a transport mechanism was proposed where the transmembrane domains diffuse through the [...] Read more.
It is poorly understood how membrane proteins destined for the inner nuclear membrane pass the crowded environment of the Nuclear Pore Complex (NPC). For the Saccharomyces cerevisiae proteins Src1/Heh1 and Heh2, a transport mechanism was proposed where the transmembrane domains diffuse through the membrane while the extralumenal domains encoding a nuclear localization signal (NLS) and intrinsically disordered linker (L) are accompanied by transport factors and travel through the NPC. Here, we validate the proposed mechanism and explore and discuss alternative interpretations of the data. First, to disprove an interpretation where the membrane proteins become membrane embedded only after nuclear import, we present biochemical and localization data to support that the previously used, as well as newly designed reporter proteins are membrane-embedded irrespective of the presence of the sorting signals, the specific transmembrane domain (multipass or tail anchored), independent of GET, and also under conditions that the proteins are trapped in the NPC. Second, using the recently established size limit for passive diffusion of membrane proteins in yeast, and using an improved assay, we confirm active import of polytopic membrane protein with extralumenal soluble domains larger than those that can pass by diffusion on similar timescales. This reinforces that NLS-L dependent active transport is distinct from passive diffusion. Thirdly, we revisit the proposed route through the center of the NPC and conclude that the previously used trapping assay is, unfortunately, poorly suited to address the route through the NPC, and the route thus remains unresolved. Apart from the uncertainty about the route through the NPC, the data confirm active, transport factor dependent, nuclear transport of membrane-embedded mono- and polytopic membrane proteins in baker’s yeast. Full article
(This article belongs to the Special Issue Nucleocytoplasmic Transport)
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Review

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1458 KiB  
Review
Complex Commingling: Nucleoporins and the Spindle Assembly Checkpoint
by Ikram Mossaid and Birthe Fahrenkrog
Cells 2015, 4(4), 706-725; https://doi.org/10.3390/cells4040706 - 03 Nov 2015
Cited by 16 | Viewed by 9073
Abstract
The segregation of the chromosomes during mitosis is an important process, in which the replicated DNA content is properly allocated into two daughter cells. To ensure their genomic integrity, cells present an essential surveillance mechanism known as the spindle assembly checkpoint (SAC), which [...] Read more.
The segregation of the chromosomes during mitosis is an important process, in which the replicated DNA content is properly allocated into two daughter cells. To ensure their genomic integrity, cells present an essential surveillance mechanism known as the spindle assembly checkpoint (SAC), which monitors the bipolar attachment of the mitotic spindle to chromosomes to prevent errors that would result in chromosome mis-segregation and aneuploidy. Multiple components of the nuclear pore complex (NPC), a gigantic protein complex that forms a channel through the nuclear envelope to allow nucleocytoplasmic exchange of macromolecules, were shown to be critical for faithful cell division and implicated in the regulation of different steps of the mitotic process, including kinetochore and spindle assembly as well as the SAC. In this review, we will describe current knowledge about the interconnection between the NPC and the SAC in an evolutional perspective, which primarily relies on the two mitotic checkpoint regulators, Mad1 and Mad2. We will further discuss the role of NPC constituents, the nucleoporins, in kinetochore and spindle assembly and the formation of the mitotic checkpoint complex during mitosis and interphase. Full article
(This article belongs to the Special Issue Nucleocytoplasmic Transport)
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3878 KiB  
Review
Structural Basis of Targeting the Exportin CRM1 in Cancer
by Achim Dickmanns, Thomas Monecke and Ralf Ficner
Cells 2015, 4(3), 538-568; https://doi.org/10.3390/cells4030538 - 21 Sep 2015
Cited by 50 | Viewed by 11087
Abstract
Recent studies have demonstrated the interference of nucleocytoplasmic trafficking with the establishment and maintenance of various cancers. Nucleocytoplasmic transport is highly regulated and coordinated, involving different nuclear transport factors or receptors, importins and exportins, that mediate cargo transport from the cytoplasm into the [...] Read more.
Recent studies have demonstrated the interference of nucleocytoplasmic trafficking with the establishment and maintenance of various cancers. Nucleocytoplasmic transport is highly regulated and coordinated, involving different nuclear transport factors or receptors, importins and exportins, that mediate cargo transport from the cytoplasm into the nucleus or the other way round, respectively. The exportin CRM1 (Chromosome region maintenance 1) exports a plethora of different protein cargoes and ribonucleoprotein complexes. Structural and biochemical analyses have enabled the deduction of individual steps of the CRM1 transport cycle. In addition, CRM1 turned out to be a valid target for anticancer drugs as it exports numerous proto-oncoproteins and tumor suppressors. Clearly, detailed understanding of the flexibility, regulatory features and cooperative binding properties of CRM1 for Ran and cargo is a prerequisite for the design of highly effective drugs. The first compound found to inhibit CRM1-dependent nuclear export was the natural drug Leptomycin B (LMB), which blocks export by competitively interacting with a highly conserved cleft on CRM1 required for nuclear export signal recognition. Clinical studies revealed serious side effects of LMB, leading to a search for alternative natural and synthetic drugs and hence a multitude of novel therapeutics. The present review examines recent progress in understanding the binding mode of natural and synthetic compounds and their inhibitory effects. Full article
(This article belongs to the Special Issue Nucleocytoplasmic Transport)
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2715 KiB  
Review
Multiple Export Mechanisms for mRNAs
by Mildred Delaleau and Katherine L. B. Borden
Cells 2015, 4(3), 452-473; https://doi.org/10.3390/cells4030452 - 28 Aug 2015
Cited by 59 | Viewed by 10909
Abstract
Nuclear mRNA export plays an important role in gene expression. We describe the mechanisms of mRNA export including the importance of mRNP assembly, docking with the nuclear basket of the nuclear pore complex (NPC), transit through the central channel of the NPC and [...] Read more.
Nuclear mRNA export plays an important role in gene expression. We describe the mechanisms of mRNA export including the importance of mRNP assembly, docking with the nuclear basket of the nuclear pore complex (NPC), transit through the central channel of the NPC and cytoplasmic release. We describe multiple mechanisms of mRNA export including NXF1 and CRM1 mediated pathways. Selective groups of mRNAs can be preferentially transported in order to respond to cellular stimuli. RNAs can be selected based on the presence of specific cis-acting RNA elements and binding of specific adaptor proteins. The role that dysregulation of this process plays in human disease is also discussed. Full article
(This article belongs to the Special Issue Nucleocytoplasmic Transport)
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1408 KiB  
Review
Spatiotemporal Regulation of Nuclear Transport Machinery and Microtubule Organization
by Naoyuki Okada and Masamitsu Sato
Cells 2015, 4(3), 406-426; https://doi.org/10.3390/cells4030406 - 21 Aug 2015
Cited by 20 | Viewed by 9247
Abstract
Spindle microtubules capture and segregate chromosomes and, therefore, their assembly is an essential event in mitosis. To carry out their mission, many key players for microtubule formation need to be strictly orchestrated. Particularly, proteins that assemble the spindle need to be translocated at [...] Read more.
Spindle microtubules capture and segregate chromosomes and, therefore, their assembly is an essential event in mitosis. To carry out their mission, many key players for microtubule formation need to be strictly orchestrated. Particularly, proteins that assemble the spindle need to be translocated at appropriate sites during mitosis. A small GTPase (hydrolase enzyme of guanosine triphosphate), Ran, controls this translocation. Ran plays many roles in many cellular events: nucleocytoplasmic shuttling through the nuclear envelope, assembly of the mitotic spindle, and reorganization of the nuclear envelope at the mitotic exit. Although these events are seemingly distinct, recent studies demonstrate that the mechanisms underlying these phenomena are substantially the same as explained by molecular interplay of the master regulator Ran, the transport factor importin, and its cargo proteins. Our review focuses on how the transport machinery regulates mitotic progression of cells. We summarize translocation mechanisms governed by Ran and its regulatory proteins, and particularly focus on Ran-GTP targets in fission yeast that promote spindle formation. We also discuss the coordination of the spatial and temporal regulation of proteins from the viewpoint of transport machinery. We propose that the transport machinery is an essential key that couples the spatial and temporal events in cells. Full article
(This article belongs to the Special Issue Nucleocytoplasmic Transport)
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1084 KiB  
Review
Nuclear Import of Yeast Proteasomes
by Julianne Burcoglu, Liang Zhao and Cordula Enenkel
Cells 2015, 4(3), 387-405; https://doi.org/10.3390/cells4030387 - 07 Aug 2015
Cited by 10 | Viewed by 7790
Abstract
Proteasomes are highly conserved protease complexes responsible for the degradation of aberrant and short-lived proteins. In highly proliferating yeast and mammalian cells, proteasomes are predominantly nuclear. During quiescence and cell cycle arrest, proteasomes accumulate in granules in close proximity to the nuclear envelope/ER. [...] Read more.
Proteasomes are highly conserved protease complexes responsible for the degradation of aberrant and short-lived proteins. In highly proliferating yeast and mammalian cells, proteasomes are predominantly nuclear. During quiescence and cell cycle arrest, proteasomes accumulate in granules in close proximity to the nuclear envelope/ER. With prolonged quiescence in yeast, these proteasome granules pinch off as membraneless organelles, and migrate as stable entities through the cytoplasm. Upon exit from quiescence, the proteasome granules clear and the proteasomes are rapidly transported into the nucleus, a process reflecting the dynamic nature of these multisubunit complexes. Due to the scarcity of studies on the nuclear transport of mammalian proteasomes, we summarised the current knowledge on the nuclear import of yeast proteasomes. This pathway uses canonical nuclear localisation signals within proteasomal subunits and Srp1/Kap95, and the canonical import receptor, named importin/karyopherin αβ. Blm10, a conserved 240 kDa protein, which is structurally related to Kap95, provides an alternative import pathway. Two models exist upon which either inactive precursor complexes or active holo-enzymes serve as the import cargo. Here, we reconcile both models and suggest that the import of inactive precursor complexes predominates in dividing cells, while the import of mature enzymes mainly occurs upon exit from quiescence. Full article
(This article belongs to the Special Issue Nucleocytoplasmic Transport)
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1169 KiB  
Review
Misdelivery at the Nuclear Pore Complex—Stopping a Virus Dead in Its Tracks
by Justin W. Flatt and Urs F. Greber
Cells 2015, 4(3), 277-296; https://doi.org/10.3390/cells4030277 - 28 Jul 2015
Cited by 36 | Viewed by 12356
Abstract
Many viruses deliver their genomes into the host cell’s nucleus before they replicate. While onco-retroviruses and papillomaviruses tether their genomes to host chromatin upon mitotic breakdown of the nuclear envelope, lentiviruses, such as human immunodeficiency virus, adenoviruses, herpesviruses, parvoviruses, influenza viruses, hepatitis B [...] Read more.
Many viruses deliver their genomes into the host cell’s nucleus before they replicate. While onco-retroviruses and papillomaviruses tether their genomes to host chromatin upon mitotic breakdown of the nuclear envelope, lentiviruses, such as human immunodeficiency virus, adenoviruses, herpesviruses, parvoviruses, influenza viruses, hepatitis B virus, polyomaviruses, and baculoviruses deliver their genomes into the nucleus of post-mitotic cells. This poses the significant challenge of slipping a DNA or RNA genome past the nuclear pore complex (NPC) embedded in the nuclear envelope. Quantitative fluorescence imaging is shedding new light on this process, with recent data implicating misdelivery of viral genomes at nuclear pores as a bottleneck to virus replication. Here, we infer NPC functions for nuclear import of viral genomes from cell biology experiments and explore potential causes of misdelivery, including improper virus docking at NPCs, incomplete translocation, virus-induced stress and innate immunity reactions. We conclude by discussing consequences of viral genome misdelivery for viruses and host cells, and lay out future questions to enhance our understanding of this phenomenon. Further studies into viral genome misdelivery may reveal unexpected aspects about NPC structure and function, as well as aid in developing strategies for controlling viral infections to improve human health. Full article
(This article belongs to the Special Issue Nucleocytoplasmic Transport)
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