The Journal of Cell Biology最新文献_第6页

Meiotic nuclear pore complex remodeling provides key insights into nuclear basket organization 减数分裂核孔复合体的重塑为核篮组织提供了关键的见解

The Journal of Cell Biology Pub Date : 2022-04-15 DOI: 10.1101/2022.04.14.488376

Grant A. King, Rahel Wettstein, Joseph M. Varberg, Keerthana Chetlapalli, M. E. Walsh, Ludovic C. Gillet, Claudia Hernandez-Armenta, P. Beltrão, R. Aebersold, S. Jaspersen, Joao Matos, E. Ünal

{"title":"Meiotic nuclear pore complex remodeling provides key insights into nuclear basket organization","authors":"Grant A. King, Rahel Wettstein, Joseph M. Varberg, Keerthana Chetlapalli, M. E. Walsh, Ludovic C. Gillet, Claudia Hernandez-Armenta, P. Beltrão, R. Aebersold, S. Jaspersen, Joao Matos, E. Ünal","doi":"10.1101/2022.04.14.488376","DOIUrl":"https://doi.org/10.1101/2022.04.14.488376","url":null,"abstract":"Nuclear pore complexes (NPCs) are large proteinaceous assemblies that mediate nuclear compartmentalization. NPCs undergo largescale structural rearrangements during mitosis in metazoans and some fungi. However, our understanding of NPC remodeling beyond mitosis remains limited. Using time-lapse fluorescence microscopy, we discovered that NPCs undergo two mechanistically-separable remodeling events during budding yeast meiosis whereby parts or all of the nuclear basket transiently dissociate from the NPC core during meiosis I and II, respectively. Meiosis I detachment, observed for Nup60 and Nup2, is driven by Polo kinase-mediated phosphorylation of Nup60 at its interface with the Y-complex. Subsequent reattachment of Nup60-Nup2 to the NPC core is mediated by a lipid-binding amphipathic helix in Nup60. Preventing Nup60-Nup2 reattachment causes misorganization of the entire nuclear basket in gametes. Strikingly, meiotic nuclear basket remodeling also occurs in the distantly related fission yeast, Schizosaccharomyces pombe. Our study reveals a conserved and developmentally programmed aspect of NPC plasticity, providing key mechanistic insights into nuclear basket organization. SUMMARY King and Wettstein et al. reveal that nuclear pore complexes undergo two distinct remodeling events during budding yeast meiosis: partial and full nuclear basket detachment. By dissecting the regulation of these events, the study provides mechanistic insights into NPC organization.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"81 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"121080202","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: 3

SNX5 targets a monoamine transporter to the TGN for assembly into dense core vesicles by AP-3 SNX5靶向单胺转运体到TGN，通过AP-3组装成致密的核心囊泡

The Journal of Cell Biology Pub Date : 2022-04-15 DOI: 10.1083/jcb.202106083

Hongfei Xu, Fei Chang, Shweta Jain, B. A. Heller, Xu Han, Yongjian Liu, R. Edwards

引用次数: 5

TRPC3 channel gating by lipids requires localization at the ER/PM junctions defined by STIM1 脂质门控TRPC3通道需要定位在STIM1定义的ER/PM连接处

The Journal of Cell Biology Pub Date : 2022-04-13 DOI: 10.1083/jcb.202107120

Haiping Liu, Wei Lin, Spencer R Leibow, Alexander J Morateck, Malini Ahuja, S. Muallem

引用次数: 11

The HOPS tethering complex is required to maintain signaling endosome identity and TORC1 activity HOPS捆绑复合物是维持信号内体身份和TORC1活性所必需的

The Journal of Cell Biology Pub Date : 2022-04-11 DOI: 10.1083/jcb.202109084

Jieqiong Gao, Raffaele Nicastro, Marie-Pierre Péli-Gulli, Sophie Grziwa, Zilei Chen, Rainer Kurre, J. Piehler, C. De Virgilio, F. Fröhlich, C. Ungermann

引用次数: 4

CPAP insufficiency leads to incomplete centrioles that duplicate but fragment CPAP功能不全导致中心粒不完整，中心粒复制但断裂

The Journal of Cell Biology Pub Date : 2022-04-11 DOI: 10.1083/jcb.202108018

A. Vásquez-Limeta, Kimberly Lukasik, Dong Kong, Catherine Sullenberger, Delgermaa Luvsanjav, Natalie Sahabandu, R. Chari, J. Loncarek

引用次数: 4

DAPLE orchestrates apical actomyosin assembly from junctional polarity complexes dple从连接极性复合体协调顶端肌动球蛋白组装

The Journal of Cell Biology Pub Date : 2022-04-07 DOI: 10.1083/jcb.202111002

A. Marivin, R. Ho, M. Garcia-Marcos

引用次数: 1

Tricellulin secures the epithelial barrier at tricellular junctions by interacting with actomyosin. 三胞蛋白通过与肌动球蛋白相互作用来保护三细胞连接处的上皮屏障。

IF 7.8

The Journal of Cell Biology Pub Date : 2022-04-04 Epub Date: 2022-02-11 DOI: 10.1083/jcb.202009037

Yuma Cho, Daichi Haraguchi, Kenta Shigetomi, Kenji Matsuzawa, Seiichi Uchida, Junichi Ikenouchi

{"title":"Tricellulin secures the epithelial barrier at tricellular junctions by interacting with actomyosin.","authors":"Yuma Cho, Daichi Haraguchi, Kenta Shigetomi, Kenji Matsuzawa, Seiichi Uchida, Junichi Ikenouchi","doi":"10.1083/jcb.202009037","DOIUrl":"https://doi.org/10.1083/jcb.202009037","url":null,"abstract":"The epithelial cell sheet functions as a barrier to prevent invasion of pathogens. It is necessary to eliminate intercellular gaps not only at bicellular junctions, but also at tricellular contacts, where three cells meet, to maintain epithelial barrier function. To that end, tight junctions between adjacent cells must associate as closely as possible, particularly at tricellular contacts. Tricellulin is an integral component of tricellular tight junctions (tTJs), but the molecular mechanism of its contribution to the epithelial barrier function remains unclear. In this study, we revealed that tricellulin contributes to barrier formation by regulating actomyosin organization at tricellular junctions. Furthermore, we identified α-catenin, which is thought to function only at adherens junctions, as a novel binding partner of tricellulin. α-catenin bridges tricellulin attachment to the bicellular actin cables that are anchored end-on at tricellular junctions. Thus, tricellulin mobilizes actomyosin contractility to close the lateral gap between the TJ strands of the three proximate cells that converge on tricellular junctions.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":" ","pages":""},"PeriodicalIF":7.8,"publicationDate":"2022-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/e0/83/JCB_202009037.PMC8847807.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39910649","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: 14

Stress-responsive regulation of extracellular proteostasis. 细胞外蛋白平衡的应激反应调节。

IF 7.8

The Journal of Cell Biology Pub Date : 2022-04-04 Epub Date: 2022-02-22 DOI: 10.1083/jcb.202112104

Jaleh S Mesgarzadeh, Joel N Buxbaum, R Luke Wiseman

{"title":"Stress-responsive regulation of extracellular proteostasis.","authors":"Jaleh S Mesgarzadeh, Joel N Buxbaum, R Luke Wiseman","doi":"10.1083/jcb.202112104","DOIUrl":"https://doi.org/10.1083/jcb.202112104","url":null,"abstract":"Genetic, environmental, and aging-related insults can promote the misfolding and subsequent aggregation of secreted proteins implicated in the pathogenesis of numerous diseases. This has led to considerable interest in understanding the molecular mechanisms responsible for regulating proteostasis in extracellular environments such as the blood and cerebrospinal fluid (CSF). Extracellular proteostasis is largely dictated by biological pathways comprising chaperones, folding enzymes, and degradation factors localized to the ER and extracellular space. These pathways limit the accumulation of nonnative, potentially aggregation-prone proteins in extracellular environments. Many reviews discuss the molecular mechanisms by which these pathways impact the conformational integrity of the secreted proteome. Here, we instead focus on describing the stress-responsive mechanisms responsible for adapting ER and extracellular proteostasis pathways to protect the secreted proteome from pathologic insults that challenge these environments. Further, we highlight new strategies to identify stress-responsive pathways involved in regulating extracellular proteostasis and describe the pathologic and therapeutic implications for these pathways in human disease.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":" ","pages":""},"PeriodicalIF":7.8,"publicationDate":"2022-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8868021/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39819022","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: 17

mTORC2 suppresses cell death induced by hypo-osmotic stress by promoting sphingomyelin transport. mTORC2通过促进鞘磷脂运输抑制低渗透应激诱导的细胞死亡。

IF 7.8

The Journal of Cell Biology Pub Date : 2022-04-04 Epub Date: 2022-03-23 DOI: 10.1083/jcb.202106160

Yumiko Ono, Kenji Matsuzawa, Junichi Ikenouchi

引用次数: 0

Filament organization of the bacterial actin MreB is dependent on the nucleotide state 细菌肌动蛋白MreB的丝组织依赖于核苷酸状态

The Journal of Cell Biology Pub Date : 2022-04-04 DOI: 10.1083/jcb.202106092

V. Pande, N. Mitra, S. Bagde, R. Srinivasan, P. Gayathri

引用次数: 8