Nucleus (Austin, Tex.)最新文献_第9页

The ESCRT-III complex is required for nuclear pore complex sequestration and regulates gamete replicative lifespan in budding yeast meiosis. 在出芽酵母减数分裂中，ESCRT-III复合体是核孔复合体隔离和调节配子复制寿命所必需的。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1812872

Bailey A Koch, Elizabeth Staley, Hui Jin, Hong-Guo Yu

{"title":"The ESCRT-III complex is required for nuclear pore complex sequestration and regulates gamete replicative lifespan in budding yeast meiosis.","authors":"Bailey A Koch, Elizabeth Staley, Hui Jin, Hong-Guo Yu","doi":"10.1080/19491034.2020.1812872","DOIUrl":"https://doi.org/10.1080/19491034.2020.1812872","url":null,"abstract":"Cellular aging occurs as a cell loses its ability to maintain homeostasis. Aging cells eliminate damaged cellular compartments and other senescence factors via self-renewal. The mechanism that regulates cellular rejuvenation remains to be further elucidated. Using budding yeast gametogenesis as a model, we show here that the endosomal sorting complex required for transport (ESCRT) III regulates nuclear envelope organization. During gametogenesis, the nuclear pore complex (NPC) and other senescence factors are sequestered away from the prospore nuclei. We show that the LEM-domain protein Heh1 (Src1) facilitates the nuclear recruitment of ESCRT-III, which is required for meiotic NPC sequestration and nuclear envelope remodeling. Furthermore, ESCRT-III-mediated nuclear reorganization appears to be critical for gamete rejuvenation, as hindering this process curtails either directly or indirectly the replicative lifespan in gametes. Our findings demonstrate the importance of ESCRT-III in nuclear envelope remodeling and its potential role in eliminating senescence factors during gametogenesis.","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"219-236"},"PeriodicalIF":0.0,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19491034.2020.1812872","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38349560","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

Impairment of nuclear F-actin formation and its relevance to cellular phenotypes in Hutchinson-Gilford progeria syndrome. 哈钦森-吉尔福德早衰综合征中核f -肌动蛋白形成损伤及其与细胞表型的相关性

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1815395

Yuto Takahashi, Shogo Hiratsuka, Nanako Machida, Daisuke Takahashi, Junpei Matsushita, Pavel Hozak, Tom Misteli, Kei Miyamoto, Masahiko Harata

{"title":"Impairment of nuclear F-actin formation and its relevance to cellular phenotypes in Hutchinson-Gilford progeria syndrome.","authors":"Yuto Takahashi, Shogo Hiratsuka, Nanako Machida, Daisuke Takahashi, Junpei Matsushita, Pavel Hozak, Tom Misteli, Kei Miyamoto, Masahiko Harata","doi":"10.1080/19491034.2020.1815395","DOIUrl":"https://doi.org/10.1080/19491034.2020.1815395","url":null,"abstract":"Hutchinson-Gilford progeria syndrome (HGPS) is a premature aging disorder caused by a mutation of lamin A, which contributes to nuclear architecture and the spatial organization of chromatin in the nucleus. The expression of a lamin A mutant, named progerin, leads to functional and structural disruption of nuclear organization. Since progerin lacks a part of the actin-binding site of lamin A, we hypothesized that nuclear actin dynamics and function are altered in HGPS cells. Nuclear F-actin is required for the organization of nuclear shape, transcriptional regulation, DNA damage repair, and activation of Wnt/β-catenin signaling. Here we show that the expression of progerin decreases nuclear F-actin and impairs F-actin-regulated transcription. When nuclear F-actin levels are increased by overexpression of nuclear-targeted actin or by using jasplakinolide, a compound that stabilizes F-actin, the irregularity of nuclear shape and defects in gene expression can be reversed. These observations provide evidence for a novel relationship between nuclear actin and the etiology of HGPS.","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"250-263"},"PeriodicalIF":0.0,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19491034.2020.1815395","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38403690","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

Nuclear lamin phosphorylation: an emerging role in gene regulation and pathogenesis of laminopathies. 核纤层蛋白磷酸化:在纤层病的基因调控和发病机制中的新作用。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1832734

Sunny Yang Liu, Kohta Ikegami

{"title":"Nuclear lamin phosphorylation: an emerging role in gene regulation and pathogenesis of laminopathies.","authors":"Sunny Yang Liu, Kohta Ikegami","doi":"10.1080/19491034.2020.1832734","DOIUrl":"https://doi.org/10.1080/19491034.2020.1832734","url":null,"abstract":"Decades of studies have established that nuclear lamin polymers form the nuclear lamina, a protein meshwork that supports the nuclear envelope structure and tethers heterochromatin to the nuclear periphery. Much less is known about unpolymerized nuclear lamins in the nuclear interior, some of which are now known to undergo specific phosphorylation. A recent finding that phosphorylated lamins bind gene enhancer regions offers a new hypothesis that lamin phosphorylation may influence transcriptional regulation in the nuclear interior. In this review, we discuss the regulation, localization, and functions of phosphorylated lamins. We summarize kinases that phosphorylate lamins in a variety of biological contexts. Our discussion extends to laminopathies, a spectrum of degenerative disorders caused by lamin gene mutations, such as cardiomyopathies and progeria. We compare the prevailing hypothesis for laminopathy pathogenesis based on lamins' function at the nuclear lamina with an emerging hypothesis based on phosphorylated lamins' function in the nuclear interior.","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"299-314"},"PeriodicalIF":0.0,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19491034.2020.1832734","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38465986","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: 34

The role of phosphorylation in the elasticity of the tethers that connect telomeres of separating anaphase chromosomes. 磷酸化在连接分离后期染色体端粒的系链弹性中的作用。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2019.1710329

Emma Kite, Arthur Forer

引用次数: 5

Reorganization of the nuclear architecture in the Drosophila melanogaster Lamin B mutant lacking the CaaX box. 缺少CaaX盒子的果蝇Lamin B突变体核结构的重组。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1819704

Semen M Bondarenko, Igor V Sharakhov

{"title":"Reorganization of the nuclear architecture in the Drosophila melanogaster Lamin B mutant lacking the CaaX box.","authors":"Semen M Bondarenko, Igor V Sharakhov","doi":"10.1080/19491034.2020.1819704","DOIUrl":"https://doi.org/10.1080/19491034.2020.1819704","url":null,"abstract":"Lamins interact with the nuclear membrane and chromatin but the precise players and mechanisms of these interactions are unknown. Here, we tested whether the removal of the CaaX motif from Lamin B disrupts its attachment to the nuclear membrane and affects chromatin distribution. We usedDrosophila melanogaster LamA25 homozygous mutants that lack the CaaX box. We found that the mutant Lamin B was not confined to the nuclear periphery but was distributed throughout the nuclear interior, colocalizing with chromosomes in salivary gland and proventriculus. The peripheral position of Lamin C, nuclear pore complex (NPC), heterochromatin protein 1a (HP1a), H3K9me2- and H3K27me3-associated chromatin remained intact. The fluorescence intensity of the DAPI-stained peripheral chromatin significantly decreased and that of the central chromatin significantly increased in the proventriculus nuclei of the mutantflies compared to wild-type. However, the mutation had little effect on chromatin radial distribution inside highly polytenized salivary gland nuclei.","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"283-298"},"PeriodicalIF":0.0,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19491034.2020.1819704","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38405789","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: 6

Advancing knowledge of the plant nuclear periphery and its application for crop science. 推进植物核外围的知识及其在作物科学中的应用。

Nucleus (Austin, Tex.) Pub Date : 2020-12-01 DOI: 10.1080/19491034.2020.1838697

David E Evans, Sarah Mermet, Christophe Tatout

{"title":"Advancing knowledge of the plant nuclear periphery and its application for crop science.","authors":"David E Evans, Sarah Mermet, Christophe Tatout","doi":"10.1080/19491034.2020.1838697","DOIUrl":"https://doi.org/10.1080/19491034.2020.1838697","url":null,"abstract":"In this review, we explore recent advances in knowledge of the structure and dynamics of the plant nuclear envelope. As a paradigm, we focused our attention on the Linker of Nucleoskeleton and Cytoskeleton (LINC) complex, a structurally conserved bridging complex comprising SUN domain proteins in the inner nuclear membrane and KASH domain proteins in the outer nuclear membrane. Studies have revealed that this bridging complex has multiple functions with structural roles in positioning the nucleus within the cell, conveying signals across the membrane and organizing chromatin in the 3D nuclear space with impact on gene transcription. We also provide an up-to-date survey in nuclear dynamics research achieved so far in the model plant Arabidopsis thaliana that highlights its potential impact on several key plant functions such as growth, seed maturation and germination, reproduction and response to biotic and abiotic stress. Finally, we bring evidences that most of the constituents of the LINC Complex and associated components are, with some specificities, conserved in monocot and dicot crop species and are displaying very similar functions to those described for Arabidopsis. This leads us to suggest that a better knowledge of this system and a better account of its potential applications will in the future enhance the resilience and productivity of crop plants.","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"11 1","pages":"347-363"},"PeriodicalIF":0.0,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19491034.2020.1838697","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38691601","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

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