Versatility at the nuclear pore complex: lessons learned from the nucleoporin Nup153

Ball, Jennifer R.; Ullman, Katharine S.

doi:10.1007/s00412-005-0019-3

Cited by 84 publications

(75 citation statements)

References 133 publications

(168 reference statements)

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“…The degradation of the nuclear basket implies cleavage of key basket proteins. In this respect, Nup153 is of particular interest due to its paramount importance for NPC structure and function and its proposed role in anchoring the NPC to the nuclear lamina (20). After induction of apoptosis in tissue culture cells, Nup153 was cleaved in a caspase-3-dependent manner and was absent from NPCs found in clusters (7, 21).…”

Section: Resultsmentioning

confidence: 99%

Apoptosis leads to a degradation of vital components of active nuclear transport and a dissociation of the nuclear lamina

Kramer

Liashkovich

Oberleithner

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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Apoptosis, a physiologically critical process, is characterized by a destruction of the cell after sequential degradation of key cellular components. Here, we set out to explore the fate of the physiologically indispensable nuclear envelope (NE) in this process. The NE mediates the critical nucleocytoplasmic transport through nuclear pore complexes (NPCs). In addition, the NE is involved in gene expression and contributes significantly to the overall structure and mechanical stability of the cell nucleus through the nuclear lamina, which underlies the entire nucleoplasmic face of the NE and thereby interconnects the NPCs, the NE, and the genomic material. Using the nano-imaging and mechanical probing approach atomic force microscopy (AFM) and biochemical methods, we unveiled the fate of the NE during apoptosis. The doomed NE sustains a degradation of both the mediators of the critical selective nucleocytoplasmic transport, namely NPC cytoplasmic filaments and basket, and the nuclear lamina. These observations are paralleled by marked softening and destabilization of the NE and the detection of vesicle-like nuclear fragments. We conclude that destruction of the cell nucleus during apoptosis proceeds in a strategic fashion. Degradation of NPC cytoplasmic filaments and basket shuts down the critical selective nucleocytoplasmic cross-talk. Degradation of the nuclear lamina disrupts the pivotal connection between the NE and the chromatin, breaks up the overall nuclear architecture, and softens the NE, thereby enabling the formation of nuclear fragments at later stages of apoptosis.atomic force microscopy ͉ nuclear envelope ͉ nuclear pores ͉ nucleocytoplasmic transport

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Section: Resultsmentioning

confidence: 99%

Apoptosis leads to a degradation of vital components of active nuclear transport and a dissociation of the nuclear lamina

Kramer

Liashkovich

Oberleithner

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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“…7C). The role of Nup153 as a scaffold likely extends to its ability to bind other participants in the nuclear import cycle as well, such as Ran and CAS (cellular apoptosis susceptibility protein) (27,28). Thus, at any one time, a limited population of Nup50 (which includes and may be restricted to the population dynamically localized to the nuclear pore) is in a local environment where factors necessary for delivery of the NLS cargo and recycling of importins ␣ and ␤ are readily accessible to facilitate this process efficiently.…”

Section: Discussionmentioning

confidence: 99%

The Nup153-Nup50 Protein Interface and Its Role in Nuclear Import

Makise

Mackay

Elgort

et al. 2012

Journal of Biological Chemistry

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Background: An interaction network involving soluble factors and nuclear pore proteins underlies nucleocytoplasmic transport. Results: Nup50 interacts with two regions of Nup153, one of which is bridged by importin ␣. Conclusion: Efficient import is dependent on the interaction between Nup153 and Nup50. Significance: Nup153 provides a scaffold to facilitate interactions that contribute to trafficking through the nuclear pore.

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“…Note that, although the zinc finger domains are resident on both faces of the pore, their precise location and arrangement within the architecture of the pore is unknown and is represented schematically here. Antibodies specific for the zinc finger region of Nup153 decorate the distal ring of the nuclear pore basket (Fahrenkrog et al, 2002), although zinc finger exposure may change during early phases of mitotic pore remodeling (Ball and Ullman, 2005).…”

Section: Discussionmentioning

confidence: 99%

Nuclear Envelope Breakdown Is Coordinated by Both Nup358/RanBP2 and Nup153, Two Nucleoporins with Zinc Finger Modules

Prunuske

Liu

Elgort

et al. 2006

MBoC

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When higher eukaryotic cells transition into mitosis, the nuclear envelope, nuclear pore complexes, and nuclear lamina are coordinately disassembled. The COPI coatomer complex, which plays a major role in membrane remodeling at the Golgi, has been implicated in the process of nuclear envelope breakdown and requires interactions at the nuclear pore complex for recruitment to this new site of action at mitosis. Nup153, a resident of the nuclear pore basket, was found to be involved in COPI recruitment, but the molecular nature of the interface between COPI and the nuclear pore has not been fully elucidated. To better understand what occurs at the nuclear pore at this juncture, we have probed the role of the nucleoporin Nup358/RanBP2. Nup358 contains a repetitive zinc finger domain with overall organization similar to a region within Nup153 that is critical to COPI association, yet inspection of these two zinc finger domains reveals features that also clearly distinguish them. Here, we found that the Nup358 zinc finger domain, but not a zinc finger domain from an unrelated protein, binds to COPI and dominantly inhibits progression of nuclear envelope breakdown in an assay that robustly recapitulates this process in vitro. Moreover, the Nup358 zinc finger domain interferes with COPI recruitment to the nuclear rim. Consistent with a role for this pore protein in coordinating nuclear envelope breakdown, Nup358-specific antibodies impair nuclear disassembly. Significantly, targeting either Nup153 or Nup358 for inhibition perturbs nuclear envelope breakdown, supporting a model in which these nucleoporins play nonredundant roles, perhaps contributing to COPI recruitment platforms on both the nuclear and cytoplasmic faces of the pore. We found that an individual zinc finger is the minimal interface for COPI association, although tandem zinc fingers are optimal. These results provide new information about the critical components of nuclear membrane remodeling and lay the foundation for a better understanding of how this process is regulated. INTRODUCTIONThe nuclear envelope creates a barrier that is critical to maintenance of the environment in the nucleus, specialized to support transcription and DNA replication. This double lipid membrane bilayer consists of an outer nuclear membrane, which is continuous with the endoplasmic reticulum (ER), and an inner nuclear membrane, which contains at least 78 different proteins, anchored via protein-protein interactions to the underlying nuclear lamina and chromatin . The nuclear envelope is perforated by nuclear pores, through which communication between the cytoplasm and nucleus occurs (Suntharalingam and Wente, 2003;Weis, 2003;Fahrenkrog et al., 2004;Pante, 2004). Despite the large size of the macromolecular nuclear pore complex (125 MDa in vertebrates), it is comprised of only ϳ30 different proteins, or nucleoporins (Nups), each present in multiple copies (Rout et al., 2000;Cronshaw et al., 2002). In metazoan cells, all these components-the lamina, nuclear pores, as well as the ...

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Versatility at the nuclear pore complex: lessons learned from the nucleoporin Nup153

Cited by 84 publications

References 133 publications

Apoptosis leads to a degradation of vital components of active nuclear transport and a dissociation of the nuclear lamina

Apoptosis leads to a degradation of vital components of active nuclear transport and a dissociation of the nuclear lamina

The Nup153-Nup50 Protein Interface and Its Role in Nuclear Import

Nuclear Envelope Breakdown Is Coordinated by Both Nup358/RanBP2 and Nup153, Two Nucleoporins with Zinc Finger Modules

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