Pore Complex Research Articles

Characterization of the Pore Network of a Cohesive Oxisol Through Morphological and Pore Complexity Analyses

Cohesive Oxisols are a type of soil common in the Coastal Plateau in Brazil. These soils represent a challenge for agriculture and their study is fundamental to better land use. There have been a few studies on the porous system of cohesive soils on the micrometer scale. Our study aimed to provide a detailed analysis of the pore complexity of the cohesive horizon of a Brazilian Oxisol using 3D images (volumetric data reconstructed by 2D CT slices) and to correlate these parameters with soil physical–hydric attributes. For this purpose, images with two different resolutions were analyzed from multifractal, lacunarity, and entropy analyses. Additionally, a characterization of hydraulic properties was carried out based on a soil water retention curve (SWRC). No differences were observed between the resolutions for the different physical parameters analyzed. The lacunarity analysis showed a greater homogeneity of the pore system with pores grouped in clusters. The multifractal analysis showed fractal characteristics for the cohesive horizon, suggesting a more homogeneous pore distribution. The main results obtained from the SWRC showed a low available water content due to the predominance of ultramicropores. Overall, the results show a less complex pore system, indicating the presence of pores of small sizes, affecting the water retention and conduction through the soil.

Genetic and clinical spectrum of steroid-resistant nephrotic syndrome with nuclear pore gene mutation.

Steroid-resistant nephrotic syndrome (SRNS) is insensitive to steroid therapy and overwhelmingly progresses to kidney failure (KF), the known pathogenic genes of which include key subunits of the nuclear pore complex (NPC), a less-recognized contributor to glomerular podocyte injury. After analyzing their clinical characterizations and obtaining parental consent, whole-exome sequencing (WES) was performed on patientswith SRNS. Several nucleoporin (NUP) biallelic pathogenic variants were identified and further analyzed by cDNA-PCR sequencing from white cells of peripheral blood, minigene assay, immunohistochemical (IHC) staining, and electron microscopy (EM) ultrastructure observation of kidney biopsy, as well as multiple in silico prediction tools, including 3D protein modeling. Here, in six familieswith SRNS, we identified pathogenic mutations in NUP85/93/107/160 genes. Specifically, thepatient with NUP93mutation developed KF six months after diagnosis at 1year 2months. Two missense mutations, c.1655A > G and c.1604A > C, disrupted the protein stability of NUP93 by IHC staining of kidney biopsy. Ultrastructurally, the above mutations led to severe vacuolization and deformed nucleus in podocytes, torn and dissolved glomerular basement membrane, and diffuse foot process effacement. Thepatient with NUP85mutation reached chronic kidney disease (CKD)stage 3 after 4years follow-up, with exons 2-5 in-frame loss and a missense variant at c.511C > T, not affecting NUP85 expression but possibly weakened interaction with Seh1. Additionally, an extended endoplasmic reticulum (ER) tubule was readily observed under EM. Meanwhile, dilated ER was also found in twochildren with NUP160mutations (c.3330 delA and c.2407 G > A; c.2241 + 1 (IVS17) G > T and c.3656T > G), one of which has undergone kidney transplantation. Compound heterozygous variants in NUP107, c.1695 G > C and c.1360 C > T, were found in a 14-year-old girl initially diagnosed with CKDstage5, with the former variant causing exon 19 skipping and early translation termination. c.1311 + 1(IVS15) G > A and c.1790 C > T were identified in the second affected girl, with the former causing exon 15 skipping and an in-frame loss of aa417-438, which disrupted the stability of NUP107 and interaction with NUP133. Our findings expand the spectrum of phenotypes and genotypes of NUPs-associated SRNS and suggest its possible pathogenic mechanism in nuclear and ER homeostasis.

NUCLEAR RNA-BINDING PROTEINS MEET CYTOPLASMIC VIRUSES.

Cytoplasmic viruses interact intricately with the nuclear pore complex and nuclear import/export machineries, affecting nuclear-cytoplasmic trafficking. This can lead to the selective accumulation of nuclear RNA-binding proteins (RBPs) in the cytoplasm. Pioneering research has shown that relocated RBPs serve as an intrinsic defence mechanism against viruses, which involves RNA export, splicing and nucleolar factors. For instance, the U2 small nuclear ribonucleoprotein (snRNP) relocates to the cytoplasm in infected cells and uses U2 snRNA to interact with viral genomes, repressing viral replication and gene expression. Here, we describe these emerging host-virus interactions and discuss the remaining questions to elucidate their antiviral mechanisms.

Nup107 contributes to the maternal to zygotic transition by preventing the premature nuclear export of pri-miRNA 427.

Emerging evidence suggests that the nuclear pore complex can have unique compositions and distinct nucleoporin functions in different cells. Here, we show that Nup107, a key component of the NPC scaffold, varies in expression over development: it is expressed at higher levels in the blastula compared to the gastrula suggesting a critical role prior to gastrulation. We find depletion of Nup107 affects the differentiation of the early germ layers leading to an expansion of the ectoderm at the expense of endoderm and mesoderm. By analyzing an RNAseq time course, we observed that depletion of Nup107 affects the maternal-zygotic transition by delaying the degradation of maternal transcripts that occurs as zygotic transcription begins. The transcripts are enriched in miR427 recognition sites, a conserved microRNA that destabilizes maternal transcripts including REST, which encodes a Kruppel-type zinc finger transcription factor that we demonstrate is critical for ectodermal cell fates. Mechanistically, we show that Nup107 is required to prevent the premature export of pri-miR427 transcript before processing. Nup107 depletion leads to the reduced production of mature miR427 and maternal transcript stabilization. We conclude that high levels of Nup107 in the early embryo are critical for the nuclear retention and subsequent processing of pri-miR427 transcripts that is required for timely maternal RNA clearance to enable gastrulation.

Cul3 substrate adaptor SPOP targets Nup153 for degradation.

SPOP is a Cul3 substrate adaptor responsible for the degradation of many proteins related to cell growth and proliferation. Because mutation or misregulation of SPOP drives cancer progression, understanding the suite of SPOP substrates is important to understanding the regulation of cell proliferation. Here, we identify Nup153, a component of the nuclear basket of the nuclear pore complex, as a novel substrate of SPOP. SPOP and Nup153 bind to each other and colocalize at the nuclear envelope and some nuclear foci in cells. The binding interaction between SPOP and Nup153 is complex and multivalent. Nup153 is ubiquitylated and degraded upon expression of SPOPWT but not its substrate binding-deficient mutant SPOPF102C. Depletion of SPOP via RNAi leads to Nup153 stabilization. Upon loss of SPOP activity, the nuclear envelope localization of spindle assembly checkpoint protein Mad1, which is tethered to the nuclear envelope by Nup153, is stronger. Altogether, our results demonstrate that SPOP regulates Nup153 levels and expands our understanding of the role of SPOP in protein and cellular homeostasis. [Media: see text] [Media: see text] [Media: see text].

Nuclear basket proteins Mlp1 and Nup2 drive heat shock-induced 3D genome restructuring.

The nuclear pore complex (NPC), a multisubunit complex located within the nuclear envelope, regulates RNA export and the import and export of proteins. Here we address the role of the NPC in driving thermal stress-induced 3D genome repositioning of Heat Shock Responsive ( HSR ) genes in yeast. We found that two nuclear basket proteins, Mlp1 and Nup2, although dispensable for NPC integrity, are required for driving HSR genes into coalesced chromatin clusters, consistent with their strong, heat shock-dependent recruitment to HSR gene regulatory and coding regions. HSR gene clustering occurs predominantly within the nucleoplasm and is independent of the essential scaffold-associated proteins Nup1 and Nup145. Notably, double depletion of Mlp1 and Nup2 has little effect on the formation of Heat Shock Factor 1 (Hsf1)-containing transcriptional condensates, Hsf1 and Pol II recruitment to HSR genes, or HSR mRNA abundance. Our results define a 3D genome restructuring role for nuclear basket proteins extrinsic to the NPC and downstream of HSR gene activation.

Interaction mapping between nucleoporins in the fission yeast Schizosaccharomyces pombe using mass-spectrometry.

Nuclear pore complexes (NPCs) act as gateways across the nuclear envelope for molecular transport between the nucleus and the cytoplasm in eukaryotes. NPCs consist of several subcomplexes formed by multiple copies of approximately 30 different proteins known as nucleoporins (Nups). In the fission yeast Schizosaccharomyces pombe, the NPC structure is unique, particularly in its outer ring subcomplexes, where the cytoplasmic and nucleoplasmic outer rings are composed of distinct sets of proteins. However, it remains unclear how this unique outer ring structure in S. pombe is supported by interactions between subcomplexes or individual Nups. In this study, we investigated protein-protein interactions between S. pombe Nups using mass spectrometry and identified Nups that interact with each subcomplex or a specific Nup. The cytoplasmic outer ring Nups bind to both the cytoplasmic filament Nups and the inner ring Nups, while the nucleoplasmic outer ring Nups bind to the nuclear basket Nups in addition to the inner ring Nups. Among the inner ring Nups, Nup155 interacts with most of the cytoplasmic and nucleoplasmic outer ring Nups, suggesting that Nup155 may serve as a hub supporting the uniquely asymmetric outer ring structure of the S. pombe NPC.

Structural basis for a nucleoporin exportin complex between RanBP2, SUMO1-RanGAP1, the E2 Ubc9, Crm1 and the Ran GTPase.

The human nucleoporin RanBP2/Nup358 interacts with SUMO1-modified RanGAP1 and the SUMO E2 Ubc9 at the nuclear pore complex (NPC) to promote export and disassembly of exportin Crm1/Ran(GTP)/cargo complexes. In mitosis, RanBP2/SUMO1-RanGAP1/Ubc9 remains intact after NPC disassembly and is recruited to kinetochores and mitotic spindles by Crm1 where it contributes to mitotic progression. Interestingly, RanBP2 binds SUMO1-RanGAP1/Ubc9 via motifs that also catalyze SUMO E3 ligase activity. Here, we resolve cryo-EM structures of a RanBP2 C-terminal fragment in complex with Crm1, SUMO1-RanGAP1/Ubc9, and two molecules of Ran(GTP). These structures reveal several unanticipated interactions with Crm1 including a nuclear export signal (NES) for RanGAP1, the deletion of which mislocalizes RanGAP1 and the Ran GTPase in cells. Our structural and biochemical results support models in which RanBP2 E3 ligase activity is dependent on Crm1, the RanGAP1 NES and Ran GTPase cycling.

CHMP2B promotes CHMP7 mediated nuclear pore complex injury in sporadic ALS

Alterations to the composition and function of neuronal nuclear pore complexes (NPCs) have been documented in multiple neurodegenerative diseases including Amyotrophic Lateral Sclerosis (ALS). Moreover, recent work has suggested that injury to the NPC can at least in part contribute to TDP-43 loss of function and mislocalization, a pathological hallmark of ALS and related neurodegenerative diseases. Collectively, these studies highlight a role for disruptions in NPC homeostasis and surveillance as a significant pathophysiologic event in neurodegeneration. The ESCRT-III nuclear surveillance pathway plays a critical role in the surveillance and maintenance of NPCs and the surrounding nuclear environment. Importantly, pathologic alterations to this pathway and its protein constituents have been implicated in neurodegenerative diseases such as ALS. However, the mechanism by which this pathway contributes to disease associated alterations in the NPC remains unknown. Here we use an induced pluripotent stem cell (iPSC) derived neuron (iPSN) model of sALS to demonstrate that CHMP7/ESCRT-III nuclear maintenance/surveillance is overactivated in sALS neurons. This overactivation is dependent upon the ESCRT-III protein CHMP2B and sustained CHMP2B dependent “activation” is sufficient to contribute to pathologic CHMP7 nuclear accumulation and POM121 reduction. Importantly, partial knockdown of CHMP2B was sufficient to alleviate NPC injury and downstream TDP-43 dysfunction in sALS neurons thereby highlighting CHMP2B as a potential therapeutic target in disease.

RRM1 promotes homologous recombination and radio/chemo-sensitivity via enhancing USP11 and E2F1-mediated RAD51AP1 transcription

Ribonucleotide reductase M1 (RRM1), the catalytic subunit of ribonucleotide reductase, plays a pivotal role in converting ribonucleotides (NTP) into deoxyribonucleotides (dNTP), essential for DNA replication and repair. Elevated RRM1 expression is associated with various human cancers, correlating with poorer prognosis and reduced overall survival rates. Our previous study found that RRM1 will enter the nucleus to promote DNA damage repair. However, the underlying mechanism remains elusive. Here, we unveil a novel role of RRM1 in promoting homologous recombination (HR) by upregulating the expression of RAD51AP1, a critical HR factor, in an E2F1-dependent manner. We demonstrate that RRM1 interacts with USP11 in the cytoplasm, and the recruitment of RRM1 to LaminB1 induced by ionizing radiation (IR) facilitates the binding of USP11 to the nuclear pore complex (NPC), promoting USP11 entry into the nucleus. Upon nuclear translocation, USP11 binds to E2F1 and inhibits the ubiquitin-mediated degradation of E2F1, thereby enhancing the transcriptional expression of RAD51AP1. Moreover, a specific RRM1 mutant lacking amino acids 731–793, crucial for its interaction with USP11 and recruitment to LaminB1, exhibits a dominant-negative effect on RAD51AP1 expression and HR. Truncations of RRM1 fail to inhibit the ubiquitin-mediated degradation of E2F1 and cannot promote the E2F1-mediated transactivation of RAD51AP1. Lastly, the full length of RRM1, not truncations, enhances tumor cells’ sensitivity to IR, underscoring its importance in radiotherapy resistance. Collectively, our results suggest a novel function of RRM1 in promoting HR-mediated DSB repair through positive regulation of RAD51AP1 transcription by direct interaction with USP11 and promoting subsequent USP11-mediated deubiquitination of E2F1. Our findings elucidate a previously unknown mechanism whereby RRM1 promotes HR-mediated DNA repair, presenting a potential therapeutic target for cancer treatment.

Novel NUP160 mutations related to simultaneous congenital nephropathy and ovarian insufficiency

Abstract Nucleoporins, as major components of nuclear pore complex, have been recently discovered to participate in organ development. Here, we report a young female patient with nephrotic proteinuria resistant to immune suppressant treatment and congenital ovarian insufficiency. Renal pathology confirmed focal segmental glomerulosclerosis (FSGS) and whole exome sequencing revealed compound heterozygous mutations in Nucleoporin 160 (NUP160), NM_015231.2 c.4154C > T(p.Pro1385Leu) and c.1102–9T > G. Notably, NUP160 mutations have been associated with congenital nephropathy in four families. We also ruled out competing genetic variants implicated in FSGS and ovarian dysgenesis. Our identification of two novel NUP160 mutations associated with congenital nephropathy and ovarian insufficiency simultaneously contributes to a deeper understanding of nuclear pore complex function in the urogenital system.

Calibration-free estimation of field dependent aberrations for single molecule localization microscopy across large fields of view.

Image quality in single molecule localization microscopy (SMLM) depends largely on the accuracy and precision of the localizations. While under ideal imaging conditions the theoretically obtainable precision and accuracy are achieved, in practice this changes if (field dependent) aberrations are present. Currently there is no simple way to measure and incorporate these aberrations into the Point Spread Function (PSF) fitting, therefore the aberrations are often taken constant or neglected all together. Here we introduce a model-based approach to estimate the field-dependent aberration directly from single molecule data without a calibration step. This is made possible by using nodal aberration theory to incorporate the field-dependency of aberrations into our fully vectorial PSF model. This results in a limited set of aberration fit parameters that can be extracted from the raw frames without a bead calibration measurement, also in retrospect. The software implementation is computationally efficient, enabling fitting of a full 2D or 3D dataset within a few minutes. We demonstrate our method on 2D and 3D localization data of microtubuli and nuclear pore complexes over fields of view (FOV) of up to 180 μm and compare it with spline-based fitting and a deep learning based approach.

NUP155 and NDC1 interaction in NSCLC: a promising target for tumor progression

BackgroundNUP155 was reported to involve breast invasive carcinoma and hepatocellular carcinoma. We hypothesized that NUP155 and NDC1impacted the progression of NSCLC.MethodsThe dataset was analyzed to find differentially expressed genes. Functional enrichment analysis and Kaplan-Meier survival analysis were performed for differentially expressed genes. Western blot, Clone formation assay, Transwell assay and CCK-8 assay were performed to determine the performance and role of the target gene in NSCLC.ResultsThe research found that the NUP family played a role in various diseases. Differential expression analysis and survival analysis were performed to identify 6 related-genes, including NUP155, NDC1, KPNA2, MAD2L1, NUP62CL, and POM121L2NUP155 and NDC1 could interact with NUP53, respectively. This effect was necessary to complete the assembly of the nuclear pore complex.ConclusionNUP155 interacted with NDC1 to complete the assembly of the nuclear pore complex, which promoted the development of NSCLC. Our study demonstrated that NUP155 was expected to be a potential target for the treatment of NSCLC.

Effects of Rock Water with Different Alkalinity and Pre-Oxidation on Re-Ignition Characteristics of Residual Coal

ABSTRACT To investigate the impact of alkaline rock water (pH = 8, 9) combined with pre-oxidation on changes in pore structure and functional groups of residual coal in goaf, and consequently, on the secondary oxidation and spontaneous combustion characteristics of coal samples, an analysis was conducted. This analysis focused on examining changes in pore morphology and functional group content of pre-oxidized coal (OI0) and water-immersed oxidized coal (OI) through experiments utilizing low-temperature nitrogen adsorption and in-situ diffuse reflectance infrared spectroscopy. Secondary oxidation and spontaneous combustion characteristics of coal samples were analyzed using thermogravimetric differential thermal analysis incorporating oxidation kinetic theory. The findings indicated that after the combined effect of pre-oxidation and alkali leaching, the mesopore volume of the coal decreased, pore complexity increased, oxygen storage capacity was enhanced, and the apparent activation energy of the coal samples was significantly reduced. This reduction in activation energy was pronounced at lower temperatures but less so at higher temperatures. Specifically, the methyl and methylene contents of OI9 were significantly higher than those of other coal samples within the temperature range of 80–160°C. Meanwhile, the heat release of the low-temperature oxidation stages of OI0, OI8, and OI9 increased by 70.82%, 190.25%, and 75.05%, respectively, compared with RC. The study indicates an elevated risk of spontaneous coal combustion following the combined treatment of alkaline leaching and pre-oxidation. This research elucidates the mechanism of spontaneous combustion of water-immersed coal by alkaline rock water and pre-oxidation, providing valuable insights for the control of coal fires in alkaline mine-water environments.

SARS-CoV-2 N protein recruits G3BP to double membrane vesicles to promote translation of viral mRNAs

Ras-GTPase-activating protein SH3-domain-binding proteins (G3BP) are critical for the formation of stress granules (SGs) through their RNA- and ribosome-binding properties. SARS-CoV-2 nucleocapsid (N) protein exhibits strong binding affinity for G3BP and inhibits infection-induced SG formation soon after infection. To study the impact of the G3BP-N interaction on viral replication and pathogenesis in detail, we generated a mutant SARS-CoV-2 (RATA) that specifically lacks the G3BP-binding motif in the N protein. RATA triggers a stronger and more persistent SG response in infected cells, showing reduced replication across various cell lines, and greatly reduced pathogenesis in K18-hACE2 transgenic mice. At early times of infection, G3BP and WT N protein strongly colocalise with dsRNA and with non-structural protein 3 (nsp3), a component of the pore complex in double membrane vesicles (DMVs) from which nascent viral RNA emerges. Furthermore, G3BP-N complexes promote highly localized translation of viral mRNAs in the immediate vicinity of the DMVs and thus contribute to efficient viral gene expression and replication. In contrast, G3BP is absent from the DMVs in cells infected with RATA and translation of viral mRNAs is less efficient. This work provides a fuller understanding of the multifunctional roles of G3BP in SARS-CoV-2 infection.

Multifunctional Roles of Sec13 Paralogues in the Euglenozoan Trypanosoma brucei.

Secretory cargos are exported from the ER via COPII coated vesicles that have an inner matrix of Sec23/Sec24 heterotetramers and an outer cage of Sec13/Sec31 heterotetramers. In addition to COPII, Sec13 is part of the nuclear pore complex (NPC) and the regulatory SEA/GATOR complex in eukaryotes, which typically have one Sec13 orthologue. The kinetoplastid parasite Trypanosoma brucei has two paralogues: TbSec13.1, an accepted component of both COPII and the NPC, and TbSec13.2. Little is known about TbSec13.2, but others have proposed that it, and its orthologue in the distantly related diplonemid Paradiplonema papillatum, operate exclusively in the SEA/GATOR complex, and that this represents an evolutionary diversification of function unique to the euglenozoan protists (doi.org/10.1098/rsob.220364). Using RNAi silencing in trypanosomes we show both TbSec13s are essential. Knockdown of each dramatically and equally delays transport of GPI-anchored secretory cargo, indicating roles for both in COPII-mediated trafficking from the ER. Immunofluorescence and proximity labeling studies confirm that both TbSec13.1 and TbSec13.2 co-localize with TbSec24.1 to ER exit sites, and thus are functional components of the COPII machinery. Our findings indicate that TbSec13.2 function is not restricted to the SEA/GATOR complex in trypanosomes.

One step 4× and 12× 3D-ExM enables robust super-resolution microscopy of nanoscale cellular structures.

Super-resolution microscopy has become an indispensable tool across diverse research fields, offering unprecedented insights into biological architectures with nanometer scale resolution. Compared with traditional nanometer-scale imaging methods such as electron microscopy, super-resolution microscopy offers several advantages, including the simultaneous labeling of multiple target biomolecules with high specificity and simpler sample preparation, making it accessible to most researchers. In this study, we introduce two optimized methods of super-resolution imaging: 4-fold and 12-fold 3D-isotropic and preserved Expansion Microscopy (4× and 12× 3D-ExM). 3D-ExM is a straightforward expansion microscopy technique featuring a single-step process, providing robust and reproducible 3D isotropic expansion for both 2D and 3D cell culture models. With standard confocal microscopy, 12× 3D-ExM achieves a lateral resolution of <30 nm, enabling the visualization of nanoscale structures, including chromosomes, kinetochores, nuclear pore complexes, and Epstein-Barr virus particles. These results demonstrate that 3D-ExM provides cost-effective and user-friendly super-resolution microscopy, making it highly suitable for a wide range of cell biology research, including studies on cellular and chromatin architectures.

TPR is required for cytoplasmic chromatin fragment formation during senescence.

During oncogene-induced senescence there are striking changes in the organisation of heterochromatin in the nucleus. This is accompanied by activation of a pro-inflammatory gene expression programme - the senescence-associated secretory phenotype (SASP) - driven by transcription factors such as NF-κB. The relationship between heterochromatin re-organisation and the SASP has been unclear. Here, we show that TPR, a protein of the nuclear pore complex basket required for heterochromatin re-organisation during senescence, is also required for the very early activation of NF-κB signalling during the stress-response phase of oncogene-induced senescence. This is prior to activation of the SASP and occurs without affecting NF-κB nuclear import. We show that TPR is required for the activation of innate immune signalling at these early stages of senescence and we link this to the formation of heterochromatin-enriched cytoplasmic chromatin fragments thought to bleb off from the nuclear periphery. We show that HMGA1 is also required for cytoplasmic chromatin fragment formation. Together these data suggest that re-organisation of heterochromatin is involved in altered structural integrity of the nuclear periphery during senescence, and that this can lead to activation of cytoplasmic nucleic acid sensing, NF-κB signalling, and activation of the SASP.

Study on the pore structure of eco-regenerated mortar using corn cob based on nuclear magnetic resonance

This study aims to investigate the influence of corn cob particles on pore structure of mortar. By using NMR technology, the pore parameters of fast-hardening sulfoaluminate cement mortar (SAC) and ordinary Portland cement mortar (PO) were measured and compared. The influence of corncob particles on the mechanical properties of eco-mortar was evaluated by uniaxial compression test. The results indicate that medium and large pores of both SAC and PO increases with corn cob particle, as well as the porosity. The fractal dimensions of harmful and multiple harmful pores are negatively correlated with the volume fraction of corn cob particles. The addition of corn cob particles reduced the overall fractal dimension of the mortar and decreased the complexity of internal pores. The probability density function of grayscale values transitions from being “thin and tall” to “short and wide”, with an increasing proportion of high grayscale values. This leads to an increase in the proportion of large pores within the mortar, resulting in a continuous deterioration of pore structure. The addition of corn cob particles greatly reduces the strength of SAC and PO, but the peak stress of SAC is higher than that of PO. When corn cob particle content is 30wt% and 50wt%, the peak stress of SAC is increased by 23.37% and 14.25%, respectively, compared with the peak stress of PO.

Nuclear pore permeability and fluid flow are modulated by its dilation state.

Changing environmental conditions necessitate rapid adaptation of cytoplasmic and nuclear volumes. We use the slime mold Dictyostelium discoideum, known for its ability to tolerate extreme changes in osmolarity, to assess which role nuclear pore complexes (NPCs) play in achieving nuclear volume adaptation and relieving mechanical stress. We capitalize on the unique properties of D.discoideum to quantify fluid flow across NPCs. D.discoideum has an elaborate NPC structure in situ. Its dilation state affects NPC permeability for nucleocytosolic flow. Based on mathematical concepts adapted from hydrodynamics, we conceptualize this phenomenon as porous flow across NPCs, which is distinct from canonically characterized modes of nucleocytoplasmic transport because of its dependence on pressure. Viral NPC blockage decreased nucleocytosolic flow. Our results may be relevant for any biological conditions that entail rapid nuclear size adaptation, including metastasizing cancer cells, migrating cells, or differentiating tissues.