The Journal of Cell Biology最新文献

BRG1 programs PRC2-complex repression and controls oligodendrocyte differentiation and remyelination. BRG1 对 PRC2 复合物的抑制进行编程，并控制少突胶质细胞的分化和再髓鞘化。

The Journal of Cell Biology Pub Date : 2024-04-23 DOI: 10.1083/jcb.202310143

Jiajia Wang, Lijun Yang, Yiwen Du, Jincheng Wang, Qinjie Weng, Xuezhao Liu, Eva Nicholson, Mei Xin, Q. R. Lu

{"title":"BRG1 programs PRC2-complex repression and controls oligodendrocyte differentiation and remyelination.","authors":"Jiajia Wang, Lijun Yang, Yiwen Du, Jincheng Wang, Qinjie Weng, Xuezhao Liu, Eva Nicholson, Mei Xin, Q. R. Lu","doi":"10.1083/jcb.202310143","DOIUrl":"https://doi.org/10.1083/jcb.202310143","url":null,"abstract":"Chromatin-remodeling protein BRG1/SMARCA4 is pivotal for establishing oligodendrocyte (OL) lineage identity. However, its functions for oligodendrocyte-precursor cell (OPC) differentiation within the postnatal brain and during remyelination remain elusive. Here, we demonstrate that Brg1 loss profoundly impairs OPC differentiation in the brain with a comparatively lesser effect in the spinal cord. Moreover, BRG1 is critical for OPC remyelination after injury. Integrative transcriptomic/genomic profiling reveals that BRG1 exhibits a dual role by promoting OPC differentiation networks while repressing OL-inhibitory cues and proneuronal programs. Furthermore, we find that BRG1 interacts with EED/PRC2 polycomb-repressive-complexes to enhance H3K27me3-mediated repression at gene loci associated with OL-differentiation inhibition and neurogenesis. Notably, BRG1 depletion decreases H3K27me3 deposition, leading to the upregulation of BMP/WNT signaling and proneurogenic genes, which suppresses OL programs. Thus, our findings reveal a hitherto unexplored spatiotemporal-specific role of BRG1 for OPC differentiation in the developing CNS and underscore a new insight into BRG1/PRC2-mediated epigenetic regulation that promotes and safeguards OL lineage commitment and differentiation.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"100 9","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140669858","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Unveiling the TRAPP: The role of plant TRAPPII in adaptive growth decisions. 揭开 TRAPP 的神秘面纱：植物 TRAPPII 在适应性生长决策中的作用。

The Journal of Cell Biology Pub Date : 2024-04-23 DOI: 10.1083/jcb.202404039

Antonio Galindo

引用次数: 0

UBAP2L ensures homeostasis of nuclear pore complexes at the intact nuclear envelope UBAP2L 确保核孔复合体在完整核膜上的平衡

The Journal of Cell Biology Pub Date : 2024-04-23 DOI: 10.1083/jcb.202310006

Yongrong Liao, Leonid Andronov, Xiaotian Liu, Junyan Lin, Lucile Guerber, Linjie Lu, Arantxa Agote-Arán, Evanthia Pangou, Li Ran, Charlotte Kleiss, Mengdi Qu, Stephane Schmucker, Luca Cirillo, Zhirong Zhang, Daniel Riveline, M. Gotta, B. Klaholz, I. Sumara

引用次数: 0

Calcium ions promote migrasome formation via Synaptotagmin-1. 钙离子通过Synaptotagmin-1促进迁移体的形成。

The Journal of Cell Biology Pub Date : 2024-04-22 DOI: 10.1083/jcb.202402060

Yiyang Han, Li Yu

引用次数: 0

Determinants of minor satellite RNA function in chromosome segregation in mouse embryonic stem cells. 小鼠胚胎干细胞染色体分离中次要卫星 RNA 功能的决定因素

The Journal of Cell Biology Pub Date : 2024-04-16 DOI: 10.1083/jcb.202309027

Yung-Li Chen, Alisha N Jones, Amy Crawford, Michael Sattler, Andreas Ettinger, M. Torres-Padilla

{"title":"Determinants of minor satellite RNA function in chromosome segregation in mouse embryonic stem cells.","authors":"Yung-Li Chen, Alisha N Jones, Amy Crawford, Michael Sattler, Andreas Ettinger, M. Torres-Padilla","doi":"10.1083/jcb.202309027","DOIUrl":"https://doi.org/10.1083/jcb.202309027","url":null,"abstract":"The centromere is a fundamental higher-order structure in chromosomes ensuring their faithful segregation upon cell division. Centromeric transcripts have been described in several species and suggested to participate in centromere function. However, low sequence conservation of centromeric repeats appears inconsistent with a role in recruiting highly conserved centromeric proteins. Here, we hypothesized that centromeric transcripts may function through a secondary structure rather than sequence conservation. Using mouse embryonic stem cells (ESCs), we show that an imbalance in the levels of forward or reverse minor satellite (MinSat) transcripts leads to severe chromosome segregation defects. We further show that MinSat RNA adopts a stem-loop secondary structure, which is conserved in human α-satellite transcripts. We identify an RNA binding region in CENPC and demonstrate that MinSat transcripts function through the structured region of the RNA. Importantly, mutants that disrupt MinSat secondary structure do not cause segregation defects. We propose that the conserved role of centromeric transcripts relies on their secondary RNA structure.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"44 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-04-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140698624","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

OMA1 clears traffic jam in TOM tunnel in mammals. OMA1 清除了哺乳动物 TOM 隧道中的交通堵塞。

The Journal of Cell Biology Pub Date : 2024-04-15 DOI: 10.1083/jcb.202403190

Shiori Sekine, Yusuke Sekine

引用次数: 0

LLPS of FXR proteins drives replication organelle clustering for β-coronaviral proliferation. FXR 蛋白的 LLPS 驱动复制细胞器集群以促进 β-冠状病毒增殖。

The Journal of Cell Biology Pub Date : 2024-04-08 DOI: 10.1083/jcb.202309140

Meng Li, Yali Hou, Yuzheng Zhou, Zhenni Yang, Hongyu Zhao, Tao Jian, Qianxi Yu, Fuxing Zeng, Xiaotian Liu, Zheng Zhang, Yan G Zhao

{"title":"LLPS of FXR proteins drives replication organelle clustering for β-coronaviral proliferation.","authors":"Meng Li, Yali Hou, Yuzheng Zhou, Zhenni Yang, Hongyu Zhao, Tao Jian, Qianxi Yu, Fuxing Zeng, Xiaotian Liu, Zheng Zhang, Yan G Zhao","doi":"10.1083/jcb.202309140","DOIUrl":"https://doi.org/10.1083/jcb.202309140","url":null,"abstract":"β-Coronaviruses remodel host endomembranes to form double-membrane vesicles (DMVs) as replication organelles (ROs) that provide a shielded microenvironment for viral RNA synthesis in infected cells. DMVs are clustered, but the molecular underpinnings and pathophysiological functions remain unknown. Here, we reveal that host fragile X-related (FXR) family proteins (FXR1/FXR2/FMR1) are required for DMV clustering induced by expression of viral non-structural proteins (Nsps) Nsp3 and Nsp4. Depleting FXRs results in DMV dispersion in the cytoplasm. FXR1/2 and FMR1 are recruited to DMV sites via specific interaction with Nsp3. FXRs form condensates driven by liquid-liquid phase separation, which is required for DMV clustering. FXR1 liquid droplets concentrate Nsp3 and Nsp3-decorated liposomes in vitro. FXR droplets facilitate recruitment of translation machinery for efficient translation surrounding DMVs. In cells depleted of FXRs, SARS-CoV-2 replication is significantly attenuated. Thus, SARS-CoV-2 exploits host FXR proteins to cluster viral DMVs via phase separation for efficient viral replication.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"22 9","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140728403","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Extracellular Caspase-1 induces hair stem cell migration in wounded and inflamed skin conditions. 细胞外 Caspase-1 可诱导毛发干细胞在受伤和发炎的皮肤条件下迁移。

The Journal of Cell Biology Pub Date : 2024-04-08 DOI: 10.1083/jcb.202306028

Akshay Hegde, Subhasri Ghosh, Akhil Shp Ananthan, Sunny Kataria, Abhik Dutta, Srilekha Prabhu, S. Khedkar, A. Dutta, Colin Jamora

引用次数: 0

The role of the AP-1 adaptor complex in outgoing and incoming membrane traffic AP-1 适配复合物在传出和传入膜交通中的作用

The Journal of Cell Biology Pub Date : 2024-04-05 DOI: 10.1083/jcb.202310071

M. S. Robinson, Robin Antrobus, Anneri Sanger, A. Davies, David C. Gershlick

引用次数: 0

Phospho-KNL-1 recognition by a TPR domain targets the BUB-1-BUB-3 complex to C. elegans kinetochores. TPR结构域对磷酸化KNL-1的识别将BUB-1-BUB-3复合物定位到优雅小鼠的动点。

The Journal of Cell Biology Pub Date : 2024-04-05 DOI: 10.1083/jcb.202402036

Jack Houston, Clémence Vissotsky, Amar Deep, Hiroyuki Hakozaki, Enice Crews, K. Oegema, Kevin D. Corbett, Pablo Lara-Gonzalez, Taekyung Kim, A. Desai

{"title":"Phospho-KNL-1 recognition by a TPR domain targets the BUB-1-BUB-3 complex to C. elegans kinetochores.","authors":"Jack Houston, Clémence Vissotsky, Amar Deep, Hiroyuki Hakozaki, Enice Crews, K. Oegema, Kevin D. Corbett, Pablo Lara-Gonzalez, Taekyung Kim, A. Desai","doi":"10.1083/jcb.202402036","DOIUrl":"https://doi.org/10.1083/jcb.202402036","url":null,"abstract":"During mitosis, the Bub1-Bub3 complex concentrates at kinetochores, the microtubule-coupling interfaces on chromosomes, where it contributes to spindle checkpoint activation, kinetochore-spindle microtubule interactions, and protection of centromeric cohesion. Bub1 has a conserved N-terminal tetratricopeptide repeat (TPR) domain followed by a binding motif for its conserved interactor Bub3. The current model for Bub1-Bub3 localization to kinetochores is that Bub3, along with its bound motif from Bub1, recognizes phosphorylated \"MELT\" motifs in the kinetochore scaffold protein Knl1. Motivated by the greater phenotypic severity of BUB-1 versus BUB-3 loss in C. elegans, we show that the BUB-1 TPR domain directly recognizes a distinct class of phosphorylated motifs in KNL-1 and that this interaction is essential for BUB-1-BUB-3 localization and function. BUB-3 recognition of phospho-MELT motifs additively contributes to drive super-stoichiometric accumulation of BUB-1-BUB-3 on its KNL-1 scaffold during mitotic entry. Bub1's TPR domain interacts with Knl1 in other species, suggesting that collaboration of TPR-dependent and Bub3-dependent interfaces in Bub1-Bub3 localization and functions may be conserved.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"17 2","pages":""},"PeriodicalIF":0.0,"publicationDate":"2024-04-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140739996","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0