Postmitotic nuclear pore assembly proceeds by radial dilation of small membrane openings

Otsuka, Shotaro; Steyer, Anna M.; Schorb, Martin; Hériché, Jean‐Karim; Hossain, M. Julius; Sethi, Suruchi; Kueblbeck, Moritz; Schwab, Yannick; Beck, Martin; Ellenberg, Jan

doi:10.1038/s41594-017-0001-9

Cited by 87 publications

(124 citation statements)

References 37 publications

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“…In this study, we showed a third model, in which fenestrations or empty holes present in the sheet‐like ER membranes are used to assemble the NPC during telophase (Figures and Supporting Information Figure S2). Our findings are consistent with those of other groups (Otsuka et al, ). Formation of fenestrations on the sheet‐like membrane is regulated by combination of types of curvature‐stabilizing proteins: reticulon family proteins, DP1/Yop1 family proteins and lunapark protein (Shemesh et al, ).…”

Section: Discussionsupporting

confidence: 94%

Roles of Nup133, Nup153 and membrane fenestrations in assembly of the nuclear pore complex at the end of mitosis

et al. 2019

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Reassembly of the nuclear pore complex (NPC) at the end of mitosis is an important event for eukaryotic nuclear function. In this study, we examined the dynamic behaviors of the endoplasmic reticulum (ER) by “Live CLEM” imaging. In metaphase, numerous fenestrations on the ER membrane were observed around chromosomes. In telophase, these fenestrations became filled at the region attached to chromosomes, whereas they remained open at the region unattached to chromosomes, suggesting that NPC assembly takes place at fenestrations on the membrane. To determine the roles of nucleoporins in postmitotic NPC formation, we used artificial beads conjugated with anti‐GFP antibody, which captures GFP‐fused proteins on the beads when incorporated into cells. Live CLEM imaging of telophase cells containing Nup133‐coated beads or Nup153‐coated beads showed that Nup133 and Nup153, as the sole effector molecules, assembled the NPC‐like structure on the membrane fenestrations. Indirect immunofluorescence staining of the Nup133‐coated beads showed that Nup133 effectively assembled Nup107 and ELYS, whereas minimal assembly of Nup98 and Nup62 was observed; the Nup153‐coated bead effectively assembled Nup98, Nup62 and Pom121, but assembled neither Nup107 nor ELYS. Our results suggest that Nup133 and Nup153 play different roles in assembling the NPC on membrane fenestrations.

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Section: Discussionsupporting

confidence: 94%

Roles of Nup133, Nup153 and membrane fenestrations in assembly of the nuclear pore complex at the end of mitosis

et al. 2019

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“…The order in which Nups assemble during postmitotic assembly has been studied in Xenopus egg extract and fixed human cells at different cell-cycle stages [88][89][90][91][92]. Additional structural insight comes from in vivo studies of rat and human cell lines [93][94][95][96]. Postmitotic assembly of NPCs happens in organisms with open mitosis upon mitotic exit, in telophase.…”

Section: Two Mechanisms Of Npc Assembly: Postmitotic Assemblymentioning

confidence: 99%

Poor old pores—The challenge of making and maintaining nuclear pore complexes in aging

2020

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The nuclear pore complex (NPC) is the sole gateway to the nuclear interior, and its function is essential to all eukaryotic life. Controlling the functionality of NPCs is a tremendous challenge for cells. Firstly, NPCs are large structures, and their complex assembly does occasionally go awry. Secondly, once assembled, some components of the NPC persist for an extremely long time and, as a result, are susceptible to accumulate damage. Lastly, a significant proportion of the NPC is composed of intrinsically disordered proteins that are prone to aggregation. In this review, we summarize how the quality of NPCs is guarded in young cells and discuss the current knowledge on the fate of NPCs during normal aging in different tissues and organisms. We discuss the extent to which current data supports a hypothesis that NPCs are poorly maintained during aging of nondividing cells, while in dividing cells the main challenge is related to the assembly of new NPCs. Our survey of current knowledge points toward NPC quality control as an important node in aging of both dividing and nondividing cells. Here, the loss of protein homeostasis during aging is central and the NPC appears to both be impacted by, and to drive, this process.

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“…These architectural units are themselves constructed from modular subcomplexes of proteins termed nucleoporins or nups that are assembled step-wise into the NE, with an emerging role for unstructured motifs that connect subcomplexes together to help build the NPC[8–10]. There remains considerable interest in understanding the biochemical and morphological differences that define post-mitotic and interphase modes of NPC assembly[11–13]. Of note, recent evidence supports that post-mitotic NPC assembly begins within small (<50 nm) pores in the reforming NE, whereas interphase NPC assembly requires an INM-ONM fusion event[12,13].…”

Section: Introductionmentioning

confidence: 99%

“…There remains considerable interest in understanding the biochemical and morphological differences that define post-mitotic and interphase modes of NPC assembly[11–13]. Of note, recent evidence supports that post-mitotic NPC assembly begins within small (<50 nm) pores in the reforming NE, whereas interphase NPC assembly requires an INM-ONM fusion event[12,13]. Interestingly, the molecular fusogen that drives INM-ONM fusion has eluded genetic (or biochemical) identification.…”

Section: Introductionmentioning

confidence: 99%

Fantastic nuclear envelope herniations and where to find them

Thaller

Lusk

2018

Biochemical Society Transactions

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Morphological abnormalities of the bounding membranes of the nucleus have long been associated with human diseases from cancer to premature aging to neurodegeneration. Studies over the past few decades support that there are both cell intrinsic and extrinsic factors (e.g. mechanical force) that can lead to nuclear envelope “herniations”, a broad catch-all term that reveals little about the underlying molecular mechanisms that contribute to these morphological defects. While there are many genetic perturbations that could ultimately change nuclear shape, here, we focus on a subset of nuclear envelope herniations that likely arise as a consequence of disrupting physiological nuclear membrane remodeling pathways required to maintain nuclear envelope homeostasis. For example, stalling of the interphase nuclear pore complex (NPC) biogenesis pathway and/or triggering of NPC quality control mechanisms can lead to herniations in budding yeast, which are remarkably similar to those observed in human disease models of early-onset dystonia. By also examining the provenance of nuclear envelope herniations associated with emerging nuclear autophagy and nuclear egress pathways, we will provide a framework to help understand the molecular pathways that contribute to nuclear deformation.

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Postmitotic nuclear pore assembly proceeds by radial dilation of small membrane openings

Cited by 87 publications

References 37 publications

Roles of Nup133, Nup153 and membrane fenestrations in assembly of the nuclear pore complex at the end of mitosis

Roles of Nup133, Nup153 and membrane fenestrations in assembly of the nuclear pore complex at the end of mitosis

Poor old pores—The challenge of making and maintaining nuclear pore complexes in aging

Fantastic nuclear envelope herniations and where to find them

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