Journal of Cell Biology最新文献_第6页

A conserved role for centriolar satellites in translation of centrosomal and ciliary proteins. 中心粒卫星在中心体和纤毛蛋白翻译中的保守作用。

IF 7.8 1区生物学

Journal of Cell Biology Pub Date : 2025-05-21 DOI: 10.1083/jcb.202408042

Claudia Pachinger,Jeroen Dobbelaere,Cornelia Rumpf-Kienzl,Shiviya Raina,Júlia Garcia-Baucells,Marina Sarantseva,Andrea Brauneis,Alexander Dammermann

{"title":"A conserved role for centriolar satellites in translation of centrosomal and ciliary proteins.","authors":"Claudia Pachinger,Jeroen Dobbelaere,Cornelia Rumpf-Kienzl,Shiviya Raina,Júlia Garcia-Baucells,Marina Sarantseva,Andrea Brauneis,Alexander Dammermann","doi":"10.1083/jcb.202408042","DOIUrl":"https://doi.org/10.1083/jcb.202408042","url":null,"abstract":"Centriolar satellites are cytoplasmic particles found in the vicinity of centrosomes and cilia whose specific functional contribution has long been unclear. Here, we identify Combover as the Drosophila ortholog of the main scaffolding component of satellites, PCM1. Like PCM1, Combover localizes to cytoplasmic foci containing centrosomal proteins and its depletion or mutation results in centrosomal and ciliary phenotypes. Strikingly, however, the concentration of satellites near centrosomes and cilia is not a conserved feature, nor do Combover foci display directed movement. Proximity interaction analysis revealed not only centrosomal and ciliary proteins, but also RNA-binding proteins and proteins involved in quality control. Further work in Drosophila and vertebrate cells found satellites to be associated with centrosomal and ciliary mRNAs, as well as evidence for protein synthesis occurring directly at satellites. Given that PCM1 depletion does not affect overall protein levels, we propose that satellites instead promote the coordinate synthesis of centrosomal and ciliary proteins, thereby facilitating the formation of protein complexes.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"31 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144103696","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Good things come in threes: Distinct C. elegans basement membranes utilize novel collagen IV trimers. 好处有三：独特的秀丽隐杆线虫基底膜利用新的胶原IV三聚体。

IF 7.8 1区生物学

Journal of Cell Biology Pub Date : 2025-05-15 DOI: 10.1083/jcb.202503175

K Elkie Peebles,Andrea Page-McCaw

引用次数: 0

The mitophagy receptors BNIP3 and NIX mediate tight attachment and expansion of the isolation membrane to mitochondria. 线粒体自噬受体BNIP3和NIX介导隔离膜与线粒体的紧密附着和扩张。

IF 7.8 1区生物学

Journal of Cell Biology Pub Date : 2025-05-13 DOI: 10.1083/jcb.202408166

Shun-Ichi Yamashita,Ritsuko Arai,Hiroshi Hada,Benjamin Scott Padman,Michael Lazarou,David C Chan,Tomotake Kanki,Satoshi Waguri

{"title":"The mitophagy receptors BNIP3 and NIX mediate tight attachment and expansion of the isolation membrane to mitochondria.","authors":"Shun-Ichi Yamashita,Ritsuko Arai,Hiroshi Hada,Benjamin Scott Padman,Michael Lazarou,David C Chan,Tomotake Kanki,Satoshi Waguri","doi":"10.1083/jcb.202408166","DOIUrl":"https://doi.org/10.1083/jcb.202408166","url":null,"abstract":"BNIP3 and NIX are the main receptors for mitophagy, but their mechanisms of action remain elusive. Here, we used correlative light EM (CLEM) and electron tomography to reveal the tight attachment of isolation membranes (IMs) to mitochondrial protrusions, often connected with ER via thin tubular and/or linear structures. In BNIP3/NIX-double knockout (DKO) HeLa cells, the ULK1 complex and nascent IM formed on mitochondria, but the IM did not expand. Artificial tethering of LC3B to mitochondria induced mitophagy that was equally efficient in DKO cells and WT cells. BNIP3 and NIX accumulated at the segregated mitochondrial protrusions via binding with LC3 through their LIR motifs but did not require dimer formation. Finally, the average distance between the IM and the mitochondrial surface in receptor-mediated mitophagy was significantly smaller than that in ubiquitin-mediated mitophagy. Collectively, these results indicate that BNIP3 and NIX are required for the tight attachment and expansion of the IM along the mitochondrial surface during mitophagy.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"35 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-05-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143945214","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Atg9 is a conserved regulator of lysosome repair. Atg9是溶酶体修复的保守调节因子。

IF 7.8 1区生物学

Journal of Cell Biology Pub Date : 2025-05-13 DOI: 10.1083/jcb.202504129

Ruoxi Wang,Eric H Baehrecke

引用次数: 0

RIM and MUNC13 membrane-binding domains are essential for neuropeptide secretion. RIM和MUNC13膜结合结构域是神经肽分泌所必需的。

IF 7.8 1区生物学

Journal of Cell Biology Pub Date : 2025-05-12 DOI: 10.1083/jcb.202409196

Fiona H Murphy,Adlin Abramian,Remco V Klaassen,Frank Koopmans,Claudia M Persoon,August B Smit,Ruud F Toonen,Matthijs Verhage

{"title":"RIM and MUNC13 membrane-binding domains are essential for neuropeptide secretion.","authors":"Fiona H Murphy,Adlin Abramian,Remco V Klaassen,Frank Koopmans,Claudia M Persoon,August B Smit,Ruud F Toonen,Matthijs Verhage","doi":"10.1083/jcb.202409196","DOIUrl":"https://doi.org/10.1083/jcb.202409196","url":null,"abstract":"Neurons release neurotransmitters from synaptic vesicles (SVs) and neuropeptides from dense-core vesicles (DCVs). The presynaptic proteins RIM and MUNC13 play key roles in both pathways. It remains unclear how DCVs are targeted to release sites and whether RIM and MUNC13 are involved in this process. Here, we show that three membrane-binding domains in RIM and MUNC13 regulate DCV exocytosis differently from SV exocytosis. Using neuropeptide secretion assays with single-vesicle resolution and peptidomics analysis of endogenous neuropeptide release in MUNC13/RIM null neurons, we demonstrate that MUNC13 is essential for DCV exocytosis. The RIM N terminus prevents MUNC13 degradation via the proteasome, and inhibiting proteasomal degradation partially rescues DCV exocytosis in RIM's absence. Unlike SV exocytosis, the PIP2-binding RIM C2B domain and MUNC13 C1-C2B polybasic face are redundant for DCV exocytosis, while the lipid-binding MUNC13 C2C domain is crucial. These results show that RIM and MUNC13 synergistically regulate DCV exocytosis through membrane interactions and reveal new mechanistic differences between SV and DCV exocytosis.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"33 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143932738","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

KIF2A stabilizes intercellular bridge microtubules to maintain mouse embryonic stem cell cytokinesis. KIF2A稳定细胞间桥微管以维持小鼠胚胎干细胞的细胞分裂。

IF 7.8 1区生物学

Journal of Cell Biology Pub Date : 2025-05-12 DOI: 10.1083/jcb.202409157

Lieke Stockmann,Hélène Kabbech,Gert-Jan Kremers,Brent van Herk,Bas Dille,Mirjam van den Hout,Wilfred F J van IJcken,Dick H W Dekkers,Jeroen A A Demmers,Ihor Smal,Danny Huylebroeck,Sreya Basu,Niels Galjart

{"title":"KIF2A stabilizes intercellular bridge microtubules to maintain mouse embryonic stem cell cytokinesis.","authors":"Lieke Stockmann,Hélène Kabbech,Gert-Jan Kremers,Brent van Herk,Bas Dille,Mirjam van den Hout,Wilfred F J van IJcken,Dick H W Dekkers,Jeroen A A Demmers,Ihor Smal,Danny Huylebroeck,Sreya Basu,Niels Galjart","doi":"10.1083/jcb.202409157","DOIUrl":"https://doi.org/10.1083/jcb.202409157","url":null,"abstract":"Cytokinesis, the final stage of cell division, serves to physically separate daughter cells. In cultured naïve mouse embryonic stem cells, cytokinesis lasts unusually long. Here, we describe a novel function for the kinesin-13 member KIF2A in this process. In genome-engineered mouse embryonic stem cells, we find that KIF2A localizes to spindle poles during metaphase and regulates spindle length in a manner consistent with its known role as a microtubule minus-end depolymerase. In contrast, during cytokinesis we observe tight binding of KIF2A to intercellular bridge microtubules. At this stage, KIF2A maintains microtubule length and number and controls microtubule acetylation. We propose that the conversion of KIF2A from a depolymerase to a stabilizer is driven by both the inhibition of its ATPase activity, which increases lattice affinity, and a preference for compacted lattices. In turn, KIF2A might maintain the compacted microtubule state at the intercellular bridge, thereby dampening acetylation. As KIF2A depletion causes pluripotency problems and affects mRNA homeostasis, our results furthermore indicate that KIF2A-mediated microtubule stabilization prolongs cytokinesis to maintain pluripotency.","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"19 1","pages":""},"PeriodicalIF":7.8,"publicationDate":"2025-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143932737","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Anillin links up with RhoA to break the symmetry of cytokinetic ring closure. 苯胺与RhoA结合，打破了细胞动力学环闭合的对称性。

IF 7.8 1区生物学

Journal of Cell Biology Pub Date : 2025-05-12 DOI: 10.1083/jcb.202504164

Guillaume D Chambaud,Vlad C Martin,Gilles R X Hickson

引用次数: 0

Ubiquitin-SUMO tag-team wrestles acute promyelocytic leukemia. 泛素- sumo标签团队对抗急性早幼粒细胞白血病。

IF 7.8 1区生物学

Journal of Cell Biology Pub Date : 2025-05-09 DOI: 10.1083/jcb.202504010

Alfred C O Vertegaal

引用次数: 0

Mechanical control of osteoclast fusion by membrane-cortex attachment and BAR proteins. 膜-皮质附着和BAR蛋白对破骨细胞融合的机械控制。

IF 7.8 1区生物学

Journal of Cell Biology Pub Date : 2025-05-08 DOI: 10.1083/jcb.202411024

Yumeng Wan,Yuri L Nemoto,Tsukasa Oikawa,Kazunori Takano,Takahiro K Fujiwara,Kazuya Tsujita,Toshiki Itoh

引用次数: 0

STIM1/2 maintain signaling competence at ER-PM contact sites during neutrophil spreading. STIM1/2在中性粒细胞扩散过程中维持ER-PM接触位点的信号传导能力。

IF 7.4 1区生物学

Journal of Cell Biology Pub Date : 2025-05-05 Epub Date: 2025-03-21 DOI: 10.1083/jcb.202406053

Camille Rabesahala de Meritens, Amado Carreras-Sureda, Nicolas Rosa, Robert Pick, Christoph Scheiermann, Nicolas Demaurex

{"title":"STIM1/2 maintain signaling competence at ER-PM contact sites during neutrophil spreading.","authors":"Camille Rabesahala de Meritens, Amado Carreras-Sureda, Nicolas Rosa, Robert Pick, Christoph Scheiermann, Nicolas Demaurex","doi":"10.1083/jcb.202406053","DOIUrl":"10.1083/jcb.202406053","url":null,"abstract":"<p><p>Neutrophils are highly motile leukocytes that migrate inside tissues to destroy invading pathogens. Ca2+ signals coordinate leukocytes migration, but whether Ca2+ fluxes mediated by Stim proteins at ER-PM contact sites regulate neutrophil actin-based motility is unclear. Here, we show that myeloid-specific Stim1/2 ablation decreases basal cytosolic Ca2+ levels and prevents adhesion-induced Ca2+ elevations in mouse neutrophils, reducing actin fiber formation and impairing spreading. Unexpectedly, more ER-PM contact sites were detected on the actin-poor adhesive membranes of Stim1/2-deficient neutrophils, which had reduced inositol-1,4,5-trisphosphate receptor (IP3R) immunoreactivity on confocal and immunogold micrographs despite preserved IP3R levels on western blots. Remarkably, Stim1/2-deficient neutrophils regained signaling and spreading competence in Ca2+-rich solutions and were recruited more effectively in mouse inflamed cremaster muscles in vivo. Our findings indicate that Stim1/2 preserve IP3R functionality in neutrophils, generating adhesion-dependent Ca2+ signals that control actin dynamics during neutrophil spreading. Stim proteins thus maintain IP3R signaling competence at adhesive membranes, enabling Ca2+-dependent actin remodeling during spreading in mouse neutrophils.</p>","PeriodicalId":15211,"journal":{"name":"Journal of Cell Biology","volume":"224 5","pages":""},"PeriodicalIF":7.4,"publicationDate":"2025-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11927589/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143673466","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0