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        <a href="/jcb/article/225/7/e202602088/282557/Chromosome-segregation-synchrony-in-S-pombe-is">
            Limits to anaphase synchrony
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        Wendi Williams, Kien Phan, Jing Chen, Stefan Legewie, Julia Kamenz, Silke Hauf
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             Chromosome segregation is triggered by separase and is abrupt and largely synchronous. Williams et al. show that synchronous chromosome segregation does not require separase-mediated positive feedback and that slight asynchrony may be unavoidable due to stochastic effects when only a few cohesin complexes remain at the time of sister chromatid separation.
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        <a href="/jcb/article/225/7/e202505012/282548/Eosinophils-promote-a-second-wave-of-postnatal">
            Eosinophils promote villus SMC development
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        Tatiana V. Petrova, Kelly de Korodi, Thea Berg, Tania Wyss, Yahya Mohammadzadeh, Lida Safazada, Kathleen Shah, Nicola L. Harris, Jeremiah Bernier-Latmani
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             Eosinophils are associated with infection and pathological fibrosis. However, healthy small intestinal villi harbor dense populations of these granulocytes. Here, Petrova et al. show that eosinophils convert PDGFRβ+ fibroblasts to specialized villus smooth muscle cells, driving a developmental program for postnatal intestinal remodeling and maturation.
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        <a href="/jcb/article/225/7/e202410019/282550/Neutrophil-serine-proteases-degrade-endothelial">
            Neutrophils degrade cortactin during extravasation
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    <div class="widget-dynamic-journal-authors">
        Idaira M. Guerrero-Fonseca, Karina B. Hernández-Almaraz, Iliana I. León-Vega, Régis Joulia, Armando Montoya-García, Hilda Vargas-Robles, Theresia E.B. Stradal, Klemens Rottner, Reyna Oregon, Eduardo Vadillo, Jennifer L. Johnson, William B. Kiosses, Sergio D. Catz, Sussan Nourshargh, Michael Schnoor
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             Guerrero-Fonseca et al. provide evidence for a cellular cross talk through which neutrophils transfer proteases into endothelial cells to degrade cortactin, thus facilitating breaching of the vascular endothelium during inflammation.
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        <a href="/jcb/article/225/7/e202411196/282313/Mitochondrially-tethered-Mmm1-can-function-as-a">
            Mmm1 as sole lipid transporter
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    <div class="widget-dynamic-journal-authors">
        Christian Covill-Cooke, Takashi Hirashima, Shin Kawano, Joe Ganellin, Andrew Moody, Sabine N.S. van Schie, Arun T. John Peter, Chika Horie Saito, Toshiya Endo, Benoît Kornmann
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    <div class="widget-dynamic-journal-teaser">
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             Covill-Cooke et al. find that the ERMES lipid-transporting complex, long-thought to be an obligate heterotetramer, can be replaced by only one component: mitochondrially tethered Mmm1.
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        May 07 2026
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            <a href="/jcb/article/225/6/e202411133/282315/Disruption-of-macrophage-cell-volume-drives">
                <img src="https://cdn.rupress.org/rup/content_public/journal/jcb/225/6/10.1083_jcb.202411133/1/s_jcb_202411133_thumb.gif?Expires=1782087111&amp;Signature=t0-QtKIUewJlM8kF9HREq7TTHxcpJ8-7cENU7FeNiKPjkdiI9e-m5p4U6WEzcJ4YnlQkRERwNSZpgD~S8nK22rwU~-EObmD6H4Z77eSlw~npnMcaf2EQ6TnSJ8iWZh6T-0PmtVhAptuoIeB1MpibBDPM8FkKNJmM~T9hg0gzTsxb4gxZMSy-~xkVX1d7iqYLxOGO00DXLDjT60iilqqPyCQh~YNxcXkMPx4rNmRcCj7EvA9FaQo~Bo7hIz3BDJmXtLYnWTz~7PaRMMBfZmIYbWJx-5tQme4gLAWJJRZMRh2otjhnUweL742xAdr-D~OYX2yu103UYtkUjZDBV8Vv9Q__&amp;Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" alt="Featured Figure" />
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        <a href="/jcb/article/225/6/e202411133/282315/Disruption-of-macrophage-cell-volume-drives">
            Cell volume disruption promotes type I interferons
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    <div class="widget-dynamic-journal-authors">
        James R. Cook, Tara A. Gleeson, Sara Gago, Stuart M. Allan, Kevin N. Couper, Catherine B. Lawrence, David Brough, Jack P. Green
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             Cook et al. show that macrophages sense cell volume disruption as a danger signal promoting transcriptional reprogramming and inflammatory responses via type I interferon signaling. Cell swelling synergizes with pathogen-sensing pathways to amplify inflammation, and macrophage volume regulation coordinates inflammatory responses during influenza infection and influences the development of the cytokine storm.
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        May 06 2026
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                <img src="https://cdn.rupress.org/rup/content_public/journal/jcb/225/7/10.1083_jcb.202306071/1/s_jcb_202306071_thumb.gif?Expires=1782087111&amp;Signature=rvX1YMOh~l6XijIpEmnYAgj3PJ64iwSxFeaZT5kAAH4F6~Zebaakkha9EfGzqup0DnImyG7r1B9ssC8ZJm1JNtH8mXfAcrGPpS4jhx2-HY7hrptcPt2~1imd8rSxyiI1Ktgaei5lyB10ICxxBb9SQM9bbcZquLwODsE~Plj4gXi5GKlK8nWBqYwbTdzHRN5rQQepLpYYk8o7WYHtsW7VWMUYe3zfD6SVP3DIMieNM0xJeLfmIYp7Kcfh-3hYybanwkkqft-3h320YHLCvHwah8kiezS-1AtgyxlHVCHArGiRGHrZYWJpLdmBqR9VPlDa9Ap0W~99hpyL4Fkzju6mjQ__&amp;Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" alt="Featured Figure" />
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        <a href="/jcb/article/225/7/e202306071/282306/Bitesize-bundles-F-actin-and-influences-actin">
            Btsz bundles actin and stabilizes membrane furrows
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    <div class="widget-dynamic-journal-authors">
        Anna R. Yeh, Gregory J. Hoeprich, Anthony D. McDougal, Bruce L. Goode, Adam C. Martin
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    <div class="widget-dynamic-journal-teaser">
        <div class="widget-dynamic-journal-teaser-inner">
             Actin network organization plays a critical role in regulating animal cell shape. We examined the <em>Drosophila</em> synaptotagmin-like protein (Btsz) in early embryo nuclear divisions, identifying a role for regulating pseudo-cleavage furrow stability. We showed that Btsz bundles actin filament networks <em>in vitro</em>.
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        May 06 2026
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            <a href="/jcb/article/225/7/e202511182/282308/NASP-functions-in-the-cytoplasm-to-prevent-histone">
                <img src="https://cdn.rupress.org/rup/content_public/journal/jcb/225/7/10.1083_jcb.202511182/1/s_jcb_202511182_thumb.gif?Expires=1782087111&amp;Signature=BWTqj5IzksVCAIHiGWDsg3WHwgPSETNPAB8lPJ~RS8CU1iMwS00D9dRSIdva7bOLAah6ipNS0Q5rpgUZkNftJT9paZBWodsKwKUgucL7FO7ucYDOWlii18ITNQWVOS51SiaeDDqfblBCFzipSAOmU-m2Yv~g-KFLOOAH6mgpEIj5A5t0bwMt3n3yau6z8JuUQy2K-55LjlKgW34k8HYnhtTmjkpgGP3CWenea9y2yW6y3uG8yKI-LLYt5yhWmvZ-bqyqPVe9pr3vzRm-zyGeXUFTDz9MOT7aLUwoYnSonmGDXphlN4k1-xVrIIKLlqq5DdlCB1F6AF5rZ6vNGzH3hA__&amp;Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" alt="Featured Figure" />
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        <a href="/jcb/article/225/7/e202511182/282308/NASP-functions-in-the-cytoplasm-to-prevent-histone">
            NASP function in early <italic>Drosophila</italic> embryogenesis
        </a>
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    <div class="widget-dynamic-journal-authors">
        Mohit Das, Eli Coronado-Chavez, Anusha D. Bhatt, Reyhaneh Tirgar, Amanda A. Amodeo, Jared T. Nordman
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        <div class="widget-dynamic-journal-teaser-inner">
             Das and Chavez et al. demonstrate that in <em>D. melanogaster</em>, the histone chaperone NASP indirectly affects the nuclear import and chromatin deposition of H3. Their findings reveal a cytoplasmic function for NASP in preventing H3 aggregation in vivo. Live imaging in <em>Drosophila</em> embryos reveals that the H3 chaperone NASP does not directly affect H3 nuclear import or export rates. Reduced H3 levels in NASP-deficient embryos indirectly affect nuclear import and H3 deposition into chromatin. In vivo, cytoplasmic NASP prevents H3 aggregation and H3 aggregation and degradation are developmentally separable events.
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