Nucleus (Austin, Tex.)最新文献_第10页

Characterization of t-loop formation by TRF2. TRF2形成t环的特征。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1783782

Leonid A Timashev, Titia De Lange

引用次数: 0

Interplay of the nuclear envelope with chromatin in physiology and pathology. 生理学和病理学中核包膜与染色质的相互作用

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1806661

Romina Burla, Mattia La Torre, Klizia Maccaroni, Fiammetta Verni, Simona Giunta, Isabella Saggio

{"title":"Interplay of the nuclear envelope with chromatin in physiology and pathology.","authors":"Romina Burla, Mattia La Torre, Klizia Maccaroni, Fiammetta Verni, Simona Giunta, Isabella Saggio","doi":"10.1080/19491034.2020.1806661","DOIUrl":"10.1080/19491034.2020.1806661","url":null,"abstract":"The nuclear envelope compartmentalizes chromatin in eukaryotic cells. The main nuclear envelope components are lamins that associate with a panoply of factors, including the LEM domain proteins. The nuclear envelope of mammalian cells opens up during cell division. It is reassembled and associated with chromatin at the end of mitosis when telomeres tether to the nuclear periphery. Lamins, LEM domain proteins, and DNA binding factors, as BAF, contribute to the reorganization of chromatin. In this context, an emerging role is that of the ESCRT complex, a machinery operating in multiple membrane assembly pathways, including nuclear envelope reformation. Research in this area is unraveling how, mechanistically, ESCRTs link to nuclear envelope associated factors as LEM domain proteins. Importantly, ESCRTs work also during interphase for repairing nuclear envelope ruptures. Altogether the advances in this field are giving new clues for the interpretation of diseases implicating nuclear envelope fragility, as laminopathies and cancer.Abbreviations: na, not analyzed; ko, knockout; kd, knockdown; NE, nuclear envelope; LEM, LAP2-emerin-MAN1 (LEM)-domain containing proteins; LINC, linker of nucleoskeleton and cytoskeleton complexes; Cyt, cytoplasm; Chr, chromatin; MB, midbody; End, endosomes; Tel, telomeres; INM, inner nuclear membrane; NP, nucleoplasm; NPC, Nuclear Pore Complex; ER, Endoplasmic Reticulum; SPB, spindle pole body.","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"205-218"},"PeriodicalIF":0.0,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/e0/93/KNCL_11_1806661.PMC7529417.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38301825","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: 0

The coordination of nuclear envelope assembly and chromosome segregation in metazoans. 后生动物核膜组装与染色体分离的协调性。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1742064

Shiwei Liu, David Pellman

引用次数: 0

Exportins can inhibit major mitotic assembly events in vitro: membrane fusion, nuclear pore formation, and spindle assembly. 输出蛋白可以抑制体外有丝分裂的主要组装事件:膜融合、核孔形成和纺锤体组装。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1798093

Matthew S Nord, Cyril Bernis, Sarah Carmona, Dennis C Garland, Anna Travesa, Douglass J Forbes

{"title":"Exportins can inhibit major mitotic assembly events in vitro: membrane fusion, nuclear pore formation, and spindle assembly.","authors":"Matthew S Nord, Cyril Bernis, Sarah Carmona, Dennis C Garland, Anna Travesa, Douglass J Forbes","doi":"10.1080/19491034.2020.1798093","DOIUrl":"https://doi.org/10.1080/19491034.2020.1798093","url":null,"abstract":"Xenopus: egg extracts are a powerful in vitro tool for studying complex biological processes, including nuclear reconstitution, nuclear membrane and pore assembly, and spindle assembly. Extracts have been further used to demonstrate a moonlighting regulatory role for nuclear import receptors or importins on these cell cycle assembly events. Here we show that exportins can also play a role in these events. Addition of Crm1, Exportin-t, or Exportin-5 decreased nuclear pore assembly in vitro. RanQ69L-GTP, a constitutively active form of RanGTP, ameliorated inhibition. Both Crm1 and Exportin-t inhibited fusion of nuclear membranes, again counteracted by RanQ69L-GTP. In mitotic extracts, Crm1 and Exportin-t negatively impacted spindle assembly. Pulldowns from the extracts using Crm1- or Exportin-t-beads revealed nucleoporins known to be essential for both nuclear pore and spindle assembly, with RanQ69L-GTP decreasing a subset of these target interactions. This study suggests a model where exportins, like importins, can regulate major mitotic assembly events.","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"178-193"},"PeriodicalIF":0.0,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19491034.2020.1798093","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38245606","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: 2

SATB1-mediated chromatin landscape in T cells. satb1介导的T细胞染色质景观。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1775037

Tomas Zelenka, Charalampos Spilianakis

引用次数: 16

Nuclear membrane ruptures, cell death, and tissue damage in the setting of nuclear lamin deficiencies. 核片层缺乏时的核膜破裂、细胞死亡和组织损伤。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1815410

Natalie Y Chen, Paul H Kim, Loren G Fong, Stephen G Young

{"title":"Nuclear membrane ruptures, cell death, and tissue damage in the setting of nuclear lamin deficiencies.","authors":"Natalie Y Chen, Paul H Kim, Loren G Fong, Stephen G Young","doi":"10.1080/19491034.2020.1815410","DOIUrl":"10.1080/19491034.2020.1815410","url":null,"abstract":"The nuclear membranes function as a barrier to separate the cell nucleus from the cytoplasm, but this barrier can be compromised by nuclear membrane ruptures, leading to intermixing of nuclear and cytoplasmic contents. Spontaneous nuclear membrane ruptures (i.e., ruptures occurring in the absence of mechanical stress) have been observed in cultured cells, but they are more frequent in the setting of defects or deficiencies in nuclear lamins and when cells are subjected to mechanical stress. Nuclear membrane ruptures in cultured cells have been linked to DNA damage, but the relevance of ruptures to developmental or physiologic processes in vivo has received little attention. Recently, we addressed that issue by examining neuronal migration in the cerebral cortex, a developmental process that subjects the cell nucleus to mechanical stress. In the setting of lamin B1 deficiency, we observed frequent nuclear membrane ruptures in migrating neurons in the developing cerebral cortex and showed that those ruptures are likely the cause of observed DNA damage, neuronal cell death, and profound neuropathology. In this review, we discuss the physiologic relevance of nuclear membrane ruptures, with a focus on migrating neurons in cell culture and in the cerebral cortex of genetically modified mice.","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"237-249"},"PeriodicalIF":0.0,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19491034.2020.1815410","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38365679","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

Emerging roles of cytoskeletal proteins in regulating gene expression and genome organization during differentiation. 细胞骨架蛋白在分化过程中调控基因表达和基因组组织中的新作用。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1742066

Xin Xie, S Raza Mahmood, Tamara Gjorgjieva, Piergiorgio Percipalle

{"title":"Emerging roles of cytoskeletal proteins in regulating gene expression and genome organization during differentiation.","authors":"Xin Xie, S Raza Mahmood, Tamara Gjorgjieva, Piergiorgio Percipalle","doi":"10.1080/19491034.2020.1742066","DOIUrl":"https://doi.org/10.1080/19491034.2020.1742066","url":null,"abstract":"In the eukaryotic cell nucleus, cytoskeletal proteins are emerging as essential players in nuclear function. In particular, actin regulates chromatin as part of ATP-dependent chromatin remodeling complexes, it modulates transcription and it is incorporated into nascent ribonucleoprotein complexes, accompanying them from the site of transcription to polyribosomes. The nuclear actin pool is undistinguishable from the cytoplasmic one in terms of its ability to undergo polymerization and it has also been implicated in the dynamics of chromatin, regulating heterochromatin segregation at the nuclear lamina and maintaining heterochromatin levels in the nuclear interiors. One of the next frontiers is, therefore, to determine a possible involvement of nuclear actin in the functional architecture of the cell nucleus by regulating the hierarchical organization of chromatin and, thus, genome organization. Here, we discuss the repertoire of these potential actin functions and how they are likely to play a role in the context of cellular differentiation.","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"53-65"},"PeriodicalIF":0.0,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19491034.2020.1742066","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37771241","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

Nuclear filaments: role in chromosomal positioning and gene expression. 核丝:在染色体定位和基因表达中的作用。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1769445

Manindra Bera, Kaushik Sengupta

{"title":"Nuclear filaments: role in chromosomal positioning and gene expression.","authors":"Manindra Bera, Kaushik Sengupta","doi":"10.1080/19491034.2020.1769445","DOIUrl":"https://doi.org/10.1080/19491034.2020.1769445","url":null,"abstract":"ABSTRACT Nuclear lamins form an elastic meshwork underlying the inner nuclear membrane and provide mechanical rigidity to the nucleus and maintain shape. Lamins also maintain chromosome positioning and play important roles in several nuclear processes like replication, DNA damage repair, transcription, and epigenetic modifications. LMNA mutations affect cardiac tissue, muscle tissues, adipose tissues to precipitate several diseases collectively termed as laminopathies. However, the rationale behind LMNA mutations and laminopathies continues to elude scientists. During interphase, several chromosomes form inter/intrachromosomal contacts inside nucleoplasm and several chromosomal loops also stretch out to make a ‘loop-cluster’ which are key players to regulate gene expressions. In this perspective, we have proposed that the lamin network in tandem with nuclear actin and myosin provide mechanical rigidity to the chromosomal contacts and facilitate loop-clusters movements. LMNA mutations thus might perturb the landscape of chromosomal contacts or loop-clusters positioning which can impair gene expression profile.","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"99-110"},"PeriodicalIF":0.0,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19491034.2020.1769445","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37976523","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

Hyperosmotic stress: in situ chromatin phase separation. 高渗胁迫:原位染色质相分离。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2019.1710321

Ada L Olins, Travis J Gould, Logan Boyd, Bettina Sarg, Donald E Olins

{"title":"Hyperosmotic stress: in situ chromatin phase separation.","authors":"Ada L Olins, Travis J Gould, Logan Boyd, Bettina Sarg, Donald E Olins","doi":"10.1080/19491034.2019.1710321","DOIUrl":"https://doi.org/10.1080/19491034.2019.1710321","url":null,"abstract":"Dehydration of cells by acute hyperosmotic stress has profound effects upon cell structure and function. Interphase chromatin and mitotic chromosomes collapse (\"congelation\"). HL-60/S4 cells remain ~100% viable for, at least, 1 hour, exhibiting shrinkage to ~2/3 their original volume, when placed in 300mM sucrose in tissue culture medium. Fixed cells were imaged by immunostaining confocal and STED microscopy. At a \"global\" structural level (μm), mitotic chromosomes congeal into a residual gel with apparent (phase) separations of Ki67, CTCF, SMC2, RAD21, H1 histones and HMG proteins. At an \"intermediate\" level (sub-μm), radial distribution analysis of STED images revealed a most probable peak DNA density separation of ~0.16 μm, essentially unchanged by hyperosmotic stress. At a \"local\" structural level (~1-2 nm), in vivo crosslinking revealed essentially unchanged crosslinked products between H1, HMG and inner histones. Hyperosmotic cellular stress is discussed in terms of concepts of mitotic chromosome structure and liquid-liquid phase separation.","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"1-18"},"PeriodicalIF":0.0,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19491034.2019.1710321","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37531731","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

Recent advances in understanding the biological roles of the plant nuclear envelope. 植物核膜生物学作用的最新研究进展。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1846836

Norman Reid Groves, Alecia Biel, Morgan Moser, Tyler Mendes, Katelyn Amstutz, Iris Meier

{"title":"Recent advances in understanding the biological roles of the plant nuclear envelope.","authors":"Norman Reid Groves, Alecia Biel, Morgan Moser, Tyler Mendes, Katelyn Amstutz, Iris Meier","doi":"10.1080/19491034.2020.1846836","DOIUrl":"10.1080/19491034.2020.1846836","url":null,"abstract":"The functional organization of the plant nuclear envelope is gaining increasing attention through new connections made between nuclear envelope-associated proteins and important plant biological processes. Animal nuclear envelope proteins play roles in nuclear morphology, nuclear anchoring and movement, chromatin tethering and mechanical signaling. However, how these roles translate to functionality in a broader biological context is often not well understood. A surprising number of plant nuclear envelope-associated proteins are plant-unique, suggesting that separate functionalities evolved after the split of Opisthokonta and Streptophyta. Significant progress has now been made in discovering broader biological roles of plant nuclear envelope proteins, increasing the number of known plant nuclear envelope proteins, and connecting known proteins to chromatin organization, gene expression, and the regulation of nuclear calcium. The interaction of viruses with the plant nuclear envelope is another emerging theme. Here, we survey the recent developments in this still relatively new, yet rapidly advancing field.","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"330-346"},"PeriodicalIF":0.0,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19491034.2020.1846836","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38576813","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