The Journal of Cell Biology最新文献_第9页

Correction: Stressed-out yeast do not pass GO. 纠正:压力过大的酵母不能通过GO。

IF 7.8

The Journal of Cell Biology Pub Date : 2022-02-07 Epub Date: 2022-01-21 DOI: 10.1083/jcb.20211103201052022c

Hilary A Coller

引用次数: 0

Actomyosin activity-dependent apical targeting of Rab11 vesicles reinforces apical constriction 肌动球蛋白活性依赖的Rab11囊泡的根尖靶向增强了根尖收缩

The Journal of Cell Biology Pub Date : 2022-01-26 DOI: 10.1083/jcb.202103069

Wei Chen, Bing He

{"title":"Actomyosin activity-dependent apical targeting of Rab11 vesicles reinforces apical constriction","authors":"Wei Chen, Bing He","doi":"10.1083/jcb.202103069","DOIUrl":"https://doi.org/10.1083/jcb.202103069","url":null,"abstract":"During tissue morphogenesis, cell shape changes resulting from cell-generated forces often require active regulation of intracellular trafficking. How mechanical stimuli influence intracellular trafficking and how such regulation impacts tissue mechanics are not fully understood. In this study, we identify an actomyosin dependent mechanism involving Rab11- mediated trafficking in regulating apical constriction in the Drosophila embryo. During Drosophila mesoderm invagination, apical actin and Myosin II (actomyosin) contractility induces apical accumulation of Rab11-marked vesicle-like structures (“Rab11 vesicles”) by promoting a directional bias in dynein mediated vesicle transport. At the apical domain, Rab11 vesicles are enriched near the adherens junctions (AJs). The apical accumulation of Rab11 vesicles is essential to prevent fragmented apical AJs, breaks in the supracellular actomyosin network and a reduction in the apical constriction rate. This Rab11 function is separate from its role in promoting apical Myosin II accumulation. These findings suggest a feedback mechanism between actomyosin activity and Rab11-mediated intracellular trafficking that regulates the force generation machinery during tissue folding.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"69 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-01-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"131993874","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

Nucleoplasmic lamin C rapidly accumulates at sites of nuclear envelope rupture with BAF and cGAS 核质层粘连蛋白C在BAF和cGAS作用下在核膜破裂部位迅速积累

The Journal of Cell Biology Pub Date : 2022-01-05 DOI: 10.1101/2022.01.05.475028

Yohei Kono, S. Adam, K. Reddy, Yixian Zheng, O. Medalia, R. Goldman, H. Kimura, T. Shimi

{"title":"Nucleoplasmic lamin C rapidly accumulates at sites of nuclear envelope rupture with BAF and cGAS","authors":"Yohei Kono, S. Adam, K. Reddy, Yixian Zheng, O. Medalia, R. Goldman, H. Kimura, T. Shimi","doi":"10.1101/2022.01.05.475028","DOIUrl":"https://doi.org/10.1101/2022.01.05.475028","url":null,"abstract":"In mammalian cell nuclei, the nuclear lamina (NL) underlies the nuclear envelope (NE) to maintain nuclear structure. The nuclear lamins, the major structural components of the NL, are involved in the protection against NE rupture induced by mechanical stress. However, the specific role of the lamins in repair of NE ruptures has not been fully determined. Our analyses using immunofluorescence and live-cell imaging revealed that lamin C but not the other lamin isoforms rapidly accumulated at sites of NE rupture induced by laser microirradiation in mouse embryonic fibroblasts. The immunoglobulin-like fold domain and the NLS were required for the recruitment from the nucleoplasm to the rupture sites with the Barrier-to-autointegration factor (BAF). The accumulation of nuclear BAF and cytoplasmic cyclic GMP-AMP synthase (cGAS) at the rupture sites was in part dependent on lamin A/C. These results suggest that nucleoplasmic lamin C, BAF and cGAS concertedly accumulate at sites of NE rupture for repair. Summary Kono et al. show the rapid recruitment of nucleoplasmic lamin C to sites of nuclear envelope rupture with Barrier-to-autointegration factor. Lamin A/C is also involved in nuclear DNA sensing with cytoplasmic cGAS at the ruptured sites.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"3 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"121764746","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: 12

Drosophila SPG12 ortholog, reticulon-like 1, governs presynaptic ER organization and Ca2+ dynamics 果蝇SPG12同源物，网状样1，控制突触前内质网组织和Ca2+动力学

The Journal of Cell Biology Pub Date : 2021-12-19 DOI: 10.1101/2021.12.17.473229

Juan J Pérez-Moreno, Rebecca C. Smith, M. Oliva, C. O’Kane

{"title":"Drosophila SPG12 ortholog, reticulon-like 1, governs presynaptic ER organization and Ca2+ dynamics","authors":"Juan J Pérez-Moreno, Rebecca C. Smith, M. Oliva, C. O’Kane","doi":"10.1101/2021.12.17.473229","DOIUrl":"https://doi.org/10.1101/2021.12.17.473229","url":null,"abstract":"Neuronal endoplasmic reticulum (ER) appears continuous throughout the cell. Its shape and continuity are influenced by ER-shaping proteins, mutations in which can cause distal axon degeneration in Hereditary Spastic Paraplegia (HSP). We therefore asked how loss of Rtnl1, a Drosophila ortholog of the human HSP gene RTN2 (SPG12), which encodes an ER-shaping protein, affects ER organization and the function of presynaptic terminals. Loss of Rtnl1 depleted ER membrane markers at Drosophila presynaptic motor terminals, and appeared to deplete narrow tubular ER while leaving cisternae largely unaffected, thus suggesting little change in resting Ca2+ storage capacity. Nevertheless, these changes were accompanied by major reductions in activity-evoked Ca2+ fluxes in the cytosol, ER lumen, and mitochondria, as well as reduced evoked and spontaneous neurotransmission. We found that reduced STIM-mediated ER-plasma membrane contacts underlie presynaptic Ca2+ defects in Rtnl1 mutants. Our results show the importance of ER architecture in presynaptic physiology and function which are therefore potential factors in the pathology of HSP.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"31 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2021-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"134172769","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: 4

Single-particle cryo-EM reveals conformational variability of the oligomeric VCC β-barrel pore in a lipid bilayer. 单粒子低温电镜显示了脂质双分子层中低聚VCC β-桶状孔的构象变异性。

IF 7.8

The Journal of Cell Biology Pub Date : 2021-12-06 Epub Date: 2021-10-07 DOI: 10.1083/jcb.202102035

Nayanika Sengupta, Anish Kumar Mondal, Suman Mishra, Kausik Chattopadhyay, Somnath Dutta

{"title":"Single-particle cryo-EM reveals conformational variability of the oligomeric VCC β-barrel pore in a lipid bilayer.","authors":"Nayanika Sengupta, Anish Kumar Mondal, Suman Mishra, Kausik Chattopadhyay, Somnath Dutta","doi":"10.1083/jcb.202102035","DOIUrl":"https://doi.org/10.1083/jcb.202102035","url":null,"abstract":"Vibrio cholerae cytolysin (VCC) is a water-soluble, membrane-damaging, pore-forming toxin (PFT) secreted by pathogenic V. cholerae, which causes eukaryotic cell death by altering the plasma membrane permeability. VCC self-assembles on the cell surface and undergoes a dramatic conformational change from prepore to heptameric pore structure. Over the past few years, several high-resolution structures of detergent-solubilized PFTs have been characterized. However, high-resolution structural characterization of small β-PFTs in a lipid environment is still rare. Therefore, we used single-particle cryo-EM to characterize the structure of the VCC oligomer in large unilamellar vesicles, which is the first atomic-resolution cryo-EM structure of VCC. From our study, we were able to provide the first documented visualization of the rim domain amino acid residues of VCC interacting with lipid membrane. Furthermore, cryo-EM characterization of lipid bilayer-embedded VCC suggests interesting conformational variabilities, especially in the transmembrane channel, which could have a potential impact on the pore architecture and assist us in understanding the pore formation mechanism.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":" ","pages":""},"PeriodicalIF":7.8,"publicationDate":"2021-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/5f/ce/JCB_202102035.PMC8504180.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39494218","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 8

Programmed cortical ER collapse drives selective ER degradation and inheritance in yeast meiosis. 程序性皮质内质网崩溃驱动酵母减数分裂中内质网的选择性降解和遗传。

IF 7.8

The Journal of Cell Biology Pub Date : 2021-12-06 Epub Date: 2021-10-18 DOI: 10.1083/jcb.202108105

George Maxwell Otto, Tia Cheunkarndee, Jessica Mae Leslie, Gloria Ann Brar

{"title":"Programmed cortical ER collapse drives selective ER degradation and inheritance in yeast meiosis.","authors":"George Maxwell Otto, Tia Cheunkarndee, Jessica Mae Leslie, Gloria Ann Brar","doi":"10.1083/jcb.202108105","DOIUrl":"https://doi.org/10.1083/jcb.202108105","url":null,"abstract":"The endoplasmic reticulum (ER) carries out essential and conserved cellular functions, which depend on the maintenance of its structure and subcellular distribution. Here, we report developmentally regulated changes in ER morphology and composition during budding yeast meiosis, a conserved differentiation program that gives rise to gametes. A subset of the cortical ER collapses away from the plasma membrane at anaphase II, thus separating into a spatially distinct compartment. This programmed collapse depends on the transcription factor Ndt80, conserved ER membrane structuring proteins Lnp1 and reticulons, and the actin cytoskeleton. A subset of ER is retained at the mother cell plasma membrane and excluded from gamete cells via the action of ER-plasma membrane tethering proteins. ER remodeling is coupled to ER degradation by selective autophagy, which relies on ER collapse and is regulated by timed expression of the autophagy receptor Atg40. Thus, developmentally programmed changes in ER morphology determine the selective degradation or inheritance of ER subdomains by gametes.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":" ","pages":""},"PeriodicalIF":7.8,"publicationDate":"2021-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8562846/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39527801","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 9

Glypican 4 mediates Wnt transport between germ layers via signaling filopodia. Glypican 4通过丝状足介导Wnt在胚层间的转运。

IF 7.8

The Journal of Cell Biology Pub Date : 2021-12-06 Epub Date: 2021-09-30 DOI: 10.1083/jcb.202009082

Bo Hu, Juan J Rodriguez, Anurag Kakkerla Balaraju, Yuanyuan Gao, Nhan T Nguyen, Heston Steen, Saeb Suhaib, Songhai Chen, Fang Lin

{"title":"Glypican 4 mediates Wnt transport between germ layers via signaling filopodia.","authors":"Bo Hu, Juan J Rodriguez, Anurag Kakkerla Balaraju, Yuanyuan Gao, Nhan T Nguyen, Heston Steen, Saeb Suhaib, Songhai Chen, Fang Lin","doi":"10.1083/jcb.202009082","DOIUrl":"https://doi.org/10.1083/jcb.202009082","url":null,"abstract":"Glypicans influence signaling pathways by regulating morphogen trafficking and reception. However, the underlying mechanisms in vertebrates are poorly understood. In zebrafish, Glypican 4 (Gpc4) is required for convergence and extension (C&E) of both the mesoderm and endoderm. Here, we show that transgenic expression of GFP-Gpc4 in the endoderm of gpc4 mutants rescued C&E defects in all germ layers. The rescue of mesoderm was likely mediated by Wnt5b and Wnt11f2 and depended on signaling filopodia rather than on cleavage of the Gpc4 GPI anchor. Gpc4 bound both Wnt5b and Wnt11f2 and regulated formation of the filopodia that transport Wnt5b and Wnt11f2 to neighboring cells. Moreover, this rescue was suppressed by blocking signaling filopodia that extend from endodermal cells. Thus, GFP-Gpc4-labeled protrusions that emanated from endodermal cells transported Wnt5b and Wnt11f2 to other germ layers, rescuing the C&E defects caused by a gpc4 deficiency. Our study reveals a new mechanism that could explain in vivo morphogen distribution involving Gpc4.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":" ","pages":""},"PeriodicalIF":7.8,"publicationDate":"2021-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/61/9f/JCB_202009082.PMC8488972.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39471910","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 12

Tubulin isotypes optimize distinct spindle positioning mechanisms during yeast mitosis. 微管蛋白同型优化不同纺锤体定位机制在酵母有丝分裂。

IF 7.8

The Journal of Cell Biology Pub Date : 2021-12-06 Epub Date: 2021-11-05 DOI: 10.1083/jcb.202010155

Emmanuel T Nsamba, Abesh Bera, Michael Costanzo, Charles Boone, Mohan L Gupta

{"title":"Tubulin isotypes optimize distinct spindle positioning mechanisms during yeast mitosis.","authors":"Emmanuel T Nsamba, Abesh Bera, Michael Costanzo, Charles Boone, Mohan L Gupta","doi":"10.1083/jcb.202010155","DOIUrl":"https://doi.org/10.1083/jcb.202010155","url":null,"abstract":"Microtubules are dynamic cytoskeleton filaments that are essential for a wide range of cellular processes. They are polymerized from tubulin, a heterodimer of α- and β-subunits. Most eukaryotic organisms express multiple isotypes of α- and β-tubulin, yet their functional relevance in any organism remains largely obscure. The two α-tubulin isotypes in budding yeast, Tub1 and Tub3, are proposed to be functionally interchangeable, yet their individual functions have not been rigorously interrogated. Here, we develop otherwise isogenic yeast strains expressing single tubulin isotypes at levels comparable to total tubulin in WT cells. Using genome-wide screening, we uncover unique interactions between the isotypes and the two major mitotic spindle positioning mechanisms. We further exploit these cells to demonstrate that Tub1 and Tub3 optimize spindle positioning by differentially recruiting key components of the Dyn1- and Kar9-dependent mechanisms, respectively. Our results provide novel mechanistic insights into how tubulin isotypes allow highly conserved microtubules to function in diverse cellular processes.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":" ","pages":""},"PeriodicalIF":7.8,"publicationDate":"2021-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/82/92/JCB_202010155.PMC8576917.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39593157","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 10

Minibrain kinase and calcineurin coordinate activity-dependent bulk endocytosis through synaptojanin. 小脑激酶和钙调磷酸酶通过突触蛋白协调活性依赖的大块内吞作用。

IF 7.8

The Journal of Cell Biology Pub Date : 2021-12-06 Epub Date: 2021-10-01 DOI: 10.1083/jcb.202011028

Yi-Jheng Peng, Junhua Geng, Ying Wu, Cristian Pinales, Jennifer Langen, Yen-Ching Chang, Christopher Buser, Karen T Chang

{"title":"Minibrain kinase and calcineurin coordinate activity-dependent bulk endocytosis through synaptojanin.","authors":"Yi-Jheng Peng, Junhua Geng, Ying Wu, Cristian Pinales, Jennifer Langen, Yen-Ching Chang, Christopher Buser, Karen T Chang","doi":"10.1083/jcb.202011028","DOIUrl":"https://doi.org/10.1083/jcb.202011028","url":null,"abstract":"Neurons use multiple modes of endocytosis, including clathrin-mediated endocytosis (CME) and activity-dependent bulk endocytosis (ADBE), during mild and intense neuronal activity, respectively, to maintain stable neurotransmission. While molecular players modulating CME are well characterized, factors regulating ADBE and mechanisms coordinating CME and ADBE activations remain poorly understood. Here we report that Minibrain/DYRK1A (Mnb), a kinase mutated in autism and up-regulated in Down's syndrome, plays a novel role in suppressing ADBE. We demonstrate that Mnb, together with calcineurin, delicately coordinates CME and ADBE by controlling the phosphoinositol phosphatase activity of synaptojanin (Synj) during varying synaptic demands. Functional domain analyses reveal that Synj's 5'-phosphoinositol phosphatase activity suppresses ADBE, while SAC1 activity is required for efficient ADBE. Consequently, Parkinson's disease mutation in Synj's SAC1 domain impairs ADBE. These data identify Mnb and Synj as novel regulators of ADBE and further indicate that CME and ADBE are differentially governed by Synj's dual phosphatase domains.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":" ","pages":""},"PeriodicalIF":7.8,"publicationDate":"2021-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/40/59/JCB_202011028.PMC8491876.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39476566","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 3

Phosphorylation and Pin1 binding to the LIC1 subunit selectively regulate mitotic dynein functions. 磷酸化和Pin1结合到LIC1亚基选择性地调节有丝分裂动力蛋白的功能。

IF 7.8

The Journal of Cell Biology Pub Date : 2021-12-06 Epub Date: 2021-10-28 DOI: 10.1083/jcb.202005184

Amrita Kumari, Chandan Kumar, Rajaiah Pergu, Megha Kumar, Sagar P Mahale, Neeraj Wasnik, Sivaram V S Mylavarapu

{"title":"Phosphorylation and Pin1 binding to the LIC1 subunit selectively regulate mitotic dynein functions.","authors":"Amrita Kumari, Chandan Kumar, Rajaiah Pergu, Megha Kumar, Sagar P Mahale, Neeraj Wasnik, Sivaram V S Mylavarapu","doi":"10.1083/jcb.202005184","DOIUrl":"https://doi.org/10.1083/jcb.202005184","url":null,"abstract":"The dynein motor performs multiple functions in mitosis by engaging with a wide cargo spectrum. One way to regulate dynein's cargo-binding selectivity is through the C-terminal domain (CTD) of its light intermediate chain 1 subunit (LIC1), which binds directly with cargo adaptors. Here we show that mitotic phosphorylation of LIC1-CTD at its three cdk1 sites is required for proper mitotic progression, for dynein loading onto prometaphase kinetochores, and for spindle assembly checkpoint inactivation in human cells. Mitotic LIC1-CTD phosphorylation also engages the prolyl isomerase Pin1 predominantly to Hook2-dynein-Nde1-Lis1 complexes, but not to dynein-spindly-dynactin complexes. LIC1-CTD dephosphorylation abrogates dynein-Pin1 binding, promotes prophase centrosome-nuclear envelope detachment, and impairs metaphase chromosome congression and mitotic Golgi fragmentation, without affecting interphase membrane transport. Phosphomutation of a conserved LIC1-CTD SP site in zebrafish leads to early developmental defects. Our work reveals that LIC1-CTD phosphorylation differentially regulates distinct mitotic dynein pools and suggests the evolutionary conservation of this phosphoregulation.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":" ","pages":""},"PeriodicalIF":7.8,"publicationDate":"2021-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/0f/40/JCB_202005184.PMC8562849.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39565860","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 7