{"title":"Calcium and magnesium deficiency induces stress granule formation to maintain magnesium homeostasis.","authors":"Tomoko Sakihara, Masatsune Tsujioka, Shinya Honda, Shigeomi Shimizu, Satoru Torii","doi":"10.1247/csf.25142","DOIUrl":"10.1247/csf.25142","url":null,"abstract":"<p><p>Hypocalcemia and hypomagnesemia frequently occur under pathological conditions such as Crohn's disease or during diuretic treatment. However, how the combined deficiency of Ca<sup>2+</sup> and Mg<sup>2+</sup> affects cellular physiology has remained unclear. In this study, we focused on this issue and found that Ca<sup>2+</sup>/Mg<sup>2+</sup> deprivation is a potent driver of stress granule (SG) formation. When SG formation was inhibited by G3BP1/2 knockdown, Ca<sup>2+</sup>/Mg<sup>2+</sup> deprivation caused a further decrease in intracellular Mg<sup>2+</sup> levels and an increase in cell death, indicating that SGs function to mitigate Mg<sup>2+</sup> loss and protect cells from death under cation-deficient conditions. Furthermore, we found that the expression of the Mg<sup>2+</sup> transporter MAGT1 is upregulated in an SG-dependent manner, and that MAGT1 knockdown further decreases intracellular Mg<sup>2+</sup> levels and increases cell death. Collectively, our results demonstrate that SG formation acts as an adaptive mechanism to maintain Mg<sup>2+</sup> homeostasis during Ca<sup>2+</sup>/Mg<sup>2+</sup> deficiency.Key words: stress granule, MAGT1, magnesium, calcium.</p>","PeriodicalId":9927,"journal":{"name":"Cell structure and function","volume":"51 1","pages":"55-65"},"PeriodicalIF":1.8,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146141206","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Tareg Omer Mohammed, Mahmoud I Shoulkamy, Djamel Eddine Chafai
{"title":"Emerging S100A11 roles: Regulation of focal adhesion dynamics and mechanosensing.","authors":"Tareg Omer Mohammed, Mahmoud I Shoulkamy, Djamel Eddine Chafai","doi":"10.1247/csf.25112","DOIUrl":"10.1247/csf.25112","url":null,"abstract":"<p><p>S100A11 is a small calcium-binding protein that has been studied in the context of growth regulation and membrane repair. However, it has recently been linked to the disassembly of focal adhesions. This new role of S100A11 has been linked to calcium influx through the stretch-activated channel Piezo1. In this review, we look at what's currently known about S100A11's structural features, interactome, and functional roles. We focus on how it responds to mechanical stress and becomes recruited to focal adhesions. We also look into its role in the disassembly of these adhesions and consider potential mechanisms. To place its activity in context, we compare S100A11 with other members of the S100 family members and discuss its contribution to calcium-dependent cytoskeletal regulation and extracellular signaling. We examine the effects of S100A11 activity in cancer metastasis, wound healing, and fibrosis. Finally, we evaluate potential ways to modulate S100A11 function for prospective therapeutic intervention. Collectively, this review projects S100A11 as a mechanosensitive calcium effector at the intersection of adhesion biology and mechanotransduction.Key words: S100A11, focal adhesions, mechanosensing, Piezo1, cytoskeleton, cell migration, cancer.</p>","PeriodicalId":9927,"journal":{"name":"Cell structure and function","volume":"51 1","pages":"11-21"},"PeriodicalIF":1.8,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145984488","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Looking back on 50 years of cell biology in Japan.","authors":"Michiyuki Matsuda","doi":"10.1247/csf.26037","DOIUrl":"10.1247/csf.26037","url":null,"abstract":"<p><p>Cell Structure and Function (CSF), the official journal of the Japan Society for Cell Biology (JSCB), celebrates its 50th anniversary in 2025. This essay traces the scientific evolution of CSF from its founding in 1975 to the present, drawing on bibliometric data retrieved from OpenAlex at ten-year intervals. Over five decades, CSF published 1,737 articles, with the Field-Weighted Citation Impact (FWCI) showing a consistent upward trend, even as total output declined following the journal's shift to electronic publication in 2005. A decade-by-decade analysis of the five most-cited articles reveals a clear evolution in research themes: early issues were dominated by plant cell biology and methodological papers in microscopy and biochemistry, while subsequent decades saw increasing focus on autophagy, the unfolded protein response, and intracellular membrane trafficking-fields in which Japanese researchers have played globally recognized pioneering roles. The turn of the millennium marked a peak in absolute citations, with landmark papers on bafilomycin A1, SNARE proteins, and a review of autophagy co-authored by Nobel Prize laureate Yoshinori Ohsumi. Two major milestones-electronic publication in 2005 and gold open-access adoption in 2016-fundamentally transformed the journal's publishing model. Looking ahead, the essay considers the role of artificial intelligence in peer review, arguing that while AI can assist in assessing novelty and reproducibility, the judgment of a manuscript's scientific significance must remain a human responsibility. CSF remains committed to disseminating reliable, foundational cell biology to the international community.Key words: Cell Structure and Function (CSF), bibliometrics, open access, artificial intelligence in peer review.</p>","PeriodicalId":9927,"journal":{"name":"Cell structure and function","volume":"51 1","pages":"i-vii"},"PeriodicalIF":1.8,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148367174","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Context-dependent interactions among afadin, ZO-1, and actin filaments.","authors":"Yuji Nitta, Satoshi Urayama, Maki Kawashima, Hayato Nakao, Takafumi Ikeda, Kazushi Higashiyama, Hatsuki Murakami, Chiyoko Kobayashi, Yuichiro Kano, Mikio Furuse, Akira Nagafuchi","doi":"10.1247/csf.25019","DOIUrl":"10.1247/csf.25019","url":null,"abstract":"<p><p>Afadin and ZO-1 are actin-binding scaffold proteins localized at cell-cell junctions. Although these proteins contain multiple protein-binding motifs for various junctional proteins, their binding partners within cells are strictly regulated. Here, we investigated the mutual interactions among afadin, ZO-1, and actin filaments using cells lacking cellular junctions derived from EL and F9 non-epithelial cells. In EL-derived cells, afadin and ZO-1 independently colocalized with various types of actin filaments. In F9-derived cells, afadin and ZO-1 colocalized as aggregates. Gene disruption analyses revealed that afadin and ZO-1 independently form aggregates in the absence of cadherin-catenin complex. Nectin-2, an afadin-binding membrane protein, was detected in afadin aggregates but not in ZO-1 aggregates, suggesting the existence of a membrane protein that binds to ZO-1. We identified this protein as JAM-C. A comparison between α-catenin-deficient and β-catenin-deficient F9 cells suggested that the extracellular domain of E-cadherin interferes with afadin and ZO-1 aggregate formation. Furthermore, gene disruption of nectin-2 suggested that JAM-C-bound ZO-1, rather than unbound ZO-1, preferentially interacts with afadin. Together, these findings indicate that interactions among afadin, ZO-1, and actin filaments are strictly regulated by various cellular contexts.Key words: afadin, ZO-1, actin, F9 cell, L cell.</p>","PeriodicalId":9927,"journal":{"name":"Cell structure and function","volume":" ","pages":"223-238"},"PeriodicalIF":1.8,"publicationDate":"2025-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12967520/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145556436","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Extracellular presentation of syntaxin4 as a potential trigger for region-specific gastrulation.","authors":"Sae Nozaki, Taisei Mihara, Yohei Hirai","doi":"10.1247/csf.25073","DOIUrl":"10.1247/csf.25073","url":null,"abstract":"<p><p>During early embryogenesis, gastrulation occurs within a specific region of the pluripotent epiblast, where cells undergo significant changes in their context. The induction of these cellular transformations in particular cell populations suggests the involvement of non-diffusible factors that activate signaling pathways in a spatiotemporal manner. Syntaxin4 (Stx4), a type IV membrane protein that functions as an intravesicular fusion mediator, often translocates across membranes to perform a latent extracellular role in locally regulating cellular behaviors. Through the culture of mouse embryonic egg cylinders isolated from E6.0 embryos and embryonic stem cells (ESCs), we demonstrate that the membrane translocation of Stx4 may play a crucial role in this early stage of development. Using membrane-impermeable antagonistic peptides against extracellular Stx4, along with several small-molecule inhibitors and activators, we found that cells with extracellular Stx4 deactivate focal adhesion kinase (FAK), which then impacts AKT/PI3K signaling and results in increased expression of P-cadherin, ultimately inducing the expression of the gastrulation marker brachyury. Activation of this signaling pathway also triggers Rho/ROCK signaling in ESCs, leading to morphological changes. These findings offer important insights into gastrulation by shedding light on the molecular mechanisms that initiate the spatiotemporal changes in the uniform pluripotent cell sheet.Key words: gastrulation, FAK, P-cadherin, Rho/ROCK, membrane flip.</p>","PeriodicalId":9927,"journal":{"name":"Cell structure and function","volume":" ","pages":"197-212"},"PeriodicalIF":1.8,"publicationDate":"2025-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12967521/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145400026","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Monitoring phospholipid dynamics in vivo with a fluorescent dye octadecyl rhodamine B.","authors":"Li Hao, Caiyi Zhao, Kuninori Suzuki","doi":"10.1247/csf.25126","DOIUrl":"10.1247/csf.25126","url":null,"abstract":"<p><p>Phospholipids are major components of biological membranes. They play an essential role in intracellular signaling and organelle dynamics; however, the availability of suitable lipid-specific probes is limited, which has hindered studies on their spatial distribution and functional dynamics in living cells. Previously, we demonstrated that octadecyl rhodamine B chloride (R18) is transported to the endoplasmic reticulum via nonvesicular membrane transport. In this study, we showed that R18 is internalized in a phosphatidylethanolamine (PE)-dependent manner in vivo. The internalization of R18 in Saccharomyces cerevisiae is blocked in PE-deficient mutants, but restored by ethanolamine supplementation, which suggests strict PE dependence. Moreover, R18 delivered to vacuoles through autophagy was not terminally retained, but underwent Pep4- and Atg15-dependent export from the vacuoles. The exported R18 was then redirected to endosomes following prolonged autophagy. These results suggest that R18 may serve as an indicator of PE dynamics and vacuole-endosome lipid transport, which contributes to lipid homeostasis inside vacuoles.Key words: autophagy, in vivo lipid dynamics, octadecyl rhodamine B (R18), phospholipase, phospholipid, vacuole, yeast.</p>","PeriodicalId":9927,"journal":{"name":"Cell structure and function","volume":" ","pages":"213-221"},"PeriodicalIF":1.8,"publicationDate":"2025-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12967523/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145437320","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Shodai Taguchi, Keita Chagi, Hiroki Kawai, Kenji Irie, Yasuyuki Suda
{"title":"Deep learning-based segmentation of 2D projection-derived overlapping prospore membrane in yeast.","authors":"Shodai Taguchi, Keita Chagi, Hiroki Kawai, Kenji Irie, Yasuyuki Suda","doi":"10.1247/csf.25032","DOIUrl":"10.1247/csf.25032","url":null,"abstract":"<p><p>Quantitative morphological analysis is crucial for understanding cellular processes. While 3D Z-stack imaging offers high-resolution data, the complexity of 3D structures makes direct interpretation and manual annotation challenging and time-consuming, especially for large datasets. Maximum Intensity Projection (MIP) is a common strategy to create more interpretable 2D representations, but this inevitably leads to artificial overlaps between structures, significantly hindering accurate automated segmentation of individual instances by conventional methods or standard deep learning tools. To address this critical challenge in 2D projection analysis, we developed DeMemSeg, a deep learning pipeline based on Mask R-CNN, specifically designed to segment overlapping membrane structures, called prospore membranes (PSMs) during yeast sporulation. DeMemSeg was trained on a custom-annotated dataset, leveraging a systematic image processing workflow. Our optimized model accurately identifies and delineates individual, overlapping PSMs, achieving segmentation performance and derived morphological measurements that are statistically indistinguishable from expert manual annotation. Notably, DeMemSeg successfully generalized to segment PSMs from unseen data acquired from gip1Δ mutant cells, capturing the distinct morphological defects in PSMs. DeMemSeg thus provides a robust, automated solution for objective quantitative analysis of complex, overlapping membrane morphologies directly from widely used 2D MIP images, offering a practical tool and adaptable workflow to advance cell biology research.Key words: deep learning-based segmentation, microscopy image processing, cellular morphology, yeast sporulation, membrane structure.</p>","PeriodicalId":9927,"journal":{"name":"Cell structure and function","volume":" ","pages":"183-195"},"PeriodicalIF":1.8,"publicationDate":"2025-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12967522/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145074360","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Supersulfides regulate cell migration in human skin keratinocytes.","authors":"Kento Kunihiro, Katsura Sano","doi":"10.1247/csf.25018","DOIUrl":"10.1247/csf.25018","url":null,"abstract":"<p><p>As the outermost organ, the skin is particularly susceptible to physical damage. Keratinocytes are a major component of the epidermis, and their migration plays a crucial role in skin wound healing. Supersulfides contribute to energy production to sustain the life activities of organisms and are anticipated to play a role in various physiological functions; however, minimal studies have investigated their presence and functions in the skin. This study aimed to determine the presence of supersulfides in the skin and investigate their effect on keratinocyte migration. Using sulfane sulfur probe 4 (SSP4), a fluorescent probe that detects sulfane sulfur, the presence of supersulfides in both skin tissue and keratinocytes was revealed. Moreover, the primary supersulfide biosynthetic enzyme, cysteinyl-tRNA synthetase 2 (CARS2), was expressed at both the tissue and cellular levels. CARS2 expression and SSP4 fluorescence intensity in keratinocytes increased during wound healing, suggesting that supersulfide is involved in the regulation of cell migration. Knockdown of CARS2 suppressed keratinocyte migration and markedly downregulated gene expression of various chemokines. Protein expression analysis revealed that supersulfides regulate E-cadherin and matrix metalloproteinase (MMP)-9 via extracellular signal-regulated kinase (ERK) and protein kinase B (Akt). Furthermore, Na<sub>2</sub>S<sub>4</sub> treatment of keratinocytes with CARS2 knockdown restored cell migration. We propose that supersulfide in the skin represents a novel mechanism of re-epithelialization and may serve as a therapeutic target for skin wounds.Key words: supersulfide, cysteinyl-tRNA synthetase 2, keratinocyte, cell migration, wound healing.</p>","PeriodicalId":9927,"journal":{"name":"Cell structure and function","volume":" ","pages":"169-182"},"PeriodicalIF":1.8,"publicationDate":"2025-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12967524/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144752539","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Assembly and mother centriole recruitment of IFT-B subcomplexes to form IFT-B holocomplex.","authors":"Koshi Tasaki, Yohei Katoh, Hye-Won Shin, Kazuhisa Nakayama","doi":"10.1247/csf.25027","DOIUrl":"10.1247/csf.25027","url":null,"abstract":"<p><p>For the biogenesis and maintenance of cilia, bidirectional protein trafficking within cilia is crucial, and is conducted by intraflagellar transport (IFT) trains containing the IFT-A and IFT-B complexes that are powered by dynein-2 and kinesin-II motors. We have recently shown that before the assembly of anterograde IFT trains, the IFT-A, IFT-B, and dynein-2 complexes are independently recruited to the mother centriole/basal body. The IFT-B complex, which consists of 16 subunits, can be divided into the IFT-B1 and IFT-B2 subcomplexes, and IFT-B1 can be further divided into the IFT-B1a and IFT-B1b subgroups. Here we investigated how the IFT-B complex is assembled and recruited to the mother centriole for ciliogenesis. Analyses using cells with knockouts of individual IFT-B subunits, and analyses of proteins coimmunoprecipitated with EGFP-fused IFT-B2, IFT-B1b, and IFT-B1a subunits expressed in these knockout cells demonstrated the following: (i) although IFT-B2 is dispensable for the linkage between IFT-B1b and IFT-B1a, it is essential for their localization to the mother centriole; (ii) IFT-B1b is essential both for bridging IFT-B2 and IFT-B1a, and for their localization to the mother centriole; (iii) IFT-B1a is not required for the linkage between IFT-B2 and IFT-B1b nor for their localization to the mother centriole; and (iv) all IFT-B components (IFT-B2, IFT-B1b, and IFT-B1a) are essential for ciliogenesis. Thus, although ciliogenesis is not a prerequisite for the recruitment of the IFT-B complex to the mother centriole, the linkage between IFT-B2 and IFT-B1b is crucial for the mother centriole localization of the IFT-B complex for ciliogenesis.Key words: cilia, ciliogenesis, distal appendages, IFT-B complex, mother centriole.</p>","PeriodicalId":9927,"journal":{"name":"Cell structure and function","volume":" ","pages":"157-168"},"PeriodicalIF":1.8,"publicationDate":"2025-07-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12967509/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144504961","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Opto-p53: A light-controllable activation of p53 signaling pathway.","authors":"Tatsuki Tsuruoka, Yuhei Goto, Kazuhiro Aoki","doi":"10.1247/csf.25017","DOIUrl":"10.1247/csf.25017","url":null,"abstract":"<p><p>p53 protein, a crucial transcription factor in cellular responses to a wide variety of stress, regulates multiple target genes involved in tumor suppression, senescence induction, and metabolic functions. To characterize the context-dependent roles of p53, it is still needed to develop an experimental system that enables selective activation of p53 in cells and tissues. In this study, we developed an optogenetic tool, Opto-p53, to control p53 signaling by light. Opto-p53 was designed to trigger p53 signaling by reconstituting p53 N-terminal and C-terminal fragments with a light-inducible dimerization (LID) system. Upon light exposure, cells expressing Opto-p53 demonstrated p53 transcriptional activation, resulting in cell death and cell cycle arrest. We further enhanced the efficacy of light-induced p53 activation by introducing specific mutations into Opto-p53 fragments. Our findings unveil the capability of Opto-p53 to serve as a powerful tool for dissecting the complex roles of p53 in cellular processes, thereby contributing to the field of synthetic biology and providing general design principles for optogenetic tools using endogenous transcription factors.Key words: synthetic biology, transcriptional factor, p53, optogenetics.</p>","PeriodicalId":9927,"journal":{"name":"Cell structure and function","volume":" ","pages":"145-156"},"PeriodicalIF":2.2,"publicationDate":"2025-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12706508/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144274286","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}