Nucleus (Austin, Tex.)Pub Date : 2024-12-01Epub Date: 2024-06-28DOI: 10.1080/19491034.2024.2373052
Ulrich Kubitscheck, Jan Peter Siebrasse
{"title":"Pre-ribosomal particles from nucleoli to cytoplasm.","authors":"Ulrich Kubitscheck, Jan Peter Siebrasse","doi":"10.1080/19491034.2024.2373052","DOIUrl":"10.1080/19491034.2024.2373052","url":null,"abstract":"<p><p>The analysis of nucleocytoplasmic transport of proteins and messenger RNA has been the focus of advanced microscopic approaches. Recently, it has been possible to identify and visualize individual pre-ribosomal particles on their way through the nuclear pore complex using both electron and light microscopy. In this review, we focused on the transport of pre-ribosomal particles in the nucleus on their way to and through the pores.</p>","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"15 1","pages":"2373052"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11216097/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141474617","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}
Nucleus (Austin, Tex.)Pub Date : 2024-12-01Epub Date: 2024-06-06DOI: 10.1080/19491034.2024.2360601
Madison E Walsh, Grant A King, Elçin Ünal
{"title":"Not just binary: embracing the complexity of nuclear division dynamics.","authors":"Madison E Walsh, Grant A King, Elçin Ünal","doi":"10.1080/19491034.2024.2360601","DOIUrl":"10.1080/19491034.2024.2360601","url":null,"abstract":"<p><p>Cell division presents a challenge for eukaryotic cells: how can chromosomes effectively segregate within the confines of a membranous nuclear compartment? Different organisms have evolved diverse solutions by modulating the degree of nuclear compartmentalization, ranging from complete nuclear envelope breakdown to complete maintenance of nuclear compartmentalization via nuclear envelope expansion. Many intermediate forms exist between these extremes, suggesting that nuclear dynamics during cell division are surprisingly plastic. In this review, we highlight the evolutionary diversity of nuclear divisions, focusing on two defining characteristics: (1) chromosome compartmentalization and (2) nucleocytoplasmic transport. Further, we highlight recent evidence that nuclear behavior during division can vary within different cellular contexts in the same organism. The variation observed within and between organisms underscores the dynamic evolution of nuclear divisions tailored to specific contexts and cellular requirements. In-depth investigation of diverse nuclear divisions will enhance our understanding of the nucleus, both in physiological and pathological states.</p>","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"15 1","pages":"2360601"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11164224/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141263495","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}
Nucleus (Austin, Tex.)Pub Date : 2024-12-01Epub Date: 2024-03-11DOI: 10.1080/19491034.2024.2325961
Jack Forman, Briar Hine, Samantha Kaonis, Soham Ghosh
{"title":"Inhibition of chromatin condensation disrupts planar cell migration.","authors":"Jack Forman, Briar Hine, Samantha Kaonis, Soham Ghosh","doi":"10.1080/19491034.2024.2325961","DOIUrl":"10.1080/19491034.2024.2325961","url":null,"abstract":"<p><p>Cell migration involves the actin cytoskeleton, and recently recognized nuclear involvement. In this study, we explore the impact of chromatin remodeling on cell migration using NIH 3T3 cells and a scratch wound assay subjected to pharmacological interventions. We inhibit histone deacetylases (HDACs) with Trichostatin A (TSA) and methyltransferase EZH2 with GSK126 to modulate chromatin compaction. Our results indicate that chromatin modifications impair wound closure efficiency, reduce individual cell migration speed, and disrupt migration persistence. Live-cell imaging reveals dynamic intranuclear chromatin remodeling and nuclear shape parameters during migration, influenced by both small- and large-scale chromatin remodeling. The altered nuclear shape is associated with disrupted cell and nuclear mechanics, suggesting a crucial interplay between chromatin remodeling, nuclear mechanics and migration. These findings shed light on the intricate connection between intranuclear chromatin dynamics, nuclear mechanics, and cell migration, providing a basis for further investigations into the molecular mechanisms governing these processes.</p>","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"15 1","pages":"2325961"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10936625/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140095340","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}
Nucleus (Austin, Tex.)Pub Date : 2024-12-01Epub Date: 2024-10-08DOI: 10.1080/19491034.2024.2400525
Lisa L Hall, Kevin M Creamer, Meg Byron, Jeanne B Lawrence
{"title":"Cytogenetic bands and sharp peaks of Alu underlie large-scale segmental regulation of nuclear genome architecture.","authors":"Lisa L Hall, Kevin M Creamer, Meg Byron, Jeanne B Lawrence","doi":"10.1080/19491034.2024.2400525","DOIUrl":"10.1080/19491034.2024.2400525","url":null,"abstract":"<p><p>Cytogenetic bands reflect genomic organization in large blocks of DNA with similar properties. Because banding patterns are invariant, this organization may often be assumed unimportant for genome regulation. Results here challenge that view. Findings here suggest cytogenetic bands reflect a visible framework upon which regulated genome architecture is built. Given Alu and L1 densities differ in cytogenetic bands, we examined their distribution after X-chromosome inactivation or formation of senescent-associated heterochromatin foci (SAHFs). Alu-rich regions remain outside both SAHFs and the Barr Body (BB), affirming that the BB is not the whole chromosome but a condensed, L1-rich core. Hi-C analysis of senescent cells demonstrates large (~10 Mb) G-bands remodel as a contiguous unit, gaining distal intrachromosomal interactions as syntenic G-bands coalesce into SAHFs. Striking peaks of Alu within R-bands strongly resist condensation. Thus, large-scale segmental genome architectur relates to dark versus light cytogenetic bands and Alu-peaks, implicating both in chromatin regulation.</p>","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"15 1","pages":"2400525"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11469423/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142395784","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}
Nucleus (Austin, Tex.)Pub Date : 2024-12-01Epub Date: 2024-05-16DOI: 10.1080/19491034.2024.2353249
Pedro A Lazo
{"title":"Nuclear functions regulated by the VRK1 kinase.","authors":"Pedro A Lazo","doi":"10.1080/19491034.2024.2353249","DOIUrl":"https://doi.org/10.1080/19491034.2024.2353249","url":null,"abstract":"<p><p>In the nucleus, the VRK1 Ser-Thr kinase is distributed in nucleoplasm and chromatin, where it has different roles. VRK1 expression increases in response to mitogenic signals. VRK1 regulates cyclin D1 expression at G0 exit and facilitates chromosome condensation at the end of G2 and G2/M progression to mitosis. These effects are mediated by the phosphorylation of histone H3 at Thr3 by VRK1, and later in mitosis by haspin. VRK1 regulates the apigenetic patterns of histones in processes requiring chromating remodeling, such as transcription, replication and DNA repair. VRK1 is overexpressed in tumors, facilitating tumor progression and resistance to genotoxic treatments. VRK1 also regulates the organization of Cajal bodies assembled on coilin, which are necessary for the assembly of different types of RNP complexes. VRK1 pathogenic variants cuase defects in Cajal bodies, functionally altering neurons with long axons and leading to neurological diseases, such as amyotrophic laterla sclerosis, spinal muscular atrophy, distal hereditay motor neuropathies and Charcot-Marie-Tooth.</p>","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"15 1","pages":"2353249"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140961119","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}
Nucleus (Austin, Tex.)Pub Date : 2024-12-01Epub Date: 2024-05-23DOI: 10.1080/19491034.2024.2352203
Yohei Kono, Takeshi Shimi
{"title":"Crosstalk between mitotic reassembly and repair of the nuclear envelope.","authors":"Yohei Kono, Takeshi Shimi","doi":"10.1080/19491034.2024.2352203","DOIUrl":"10.1080/19491034.2024.2352203","url":null,"abstract":"<p><p>In eukaryotic cells, the nuclear envelope (NE) is a membrane partition between the nucleus and the cytoplasm to compartmentalize nuclear contents. It plays an important role in facilitating nuclear functions including transcription, DNA replication and repair. In mammalian cells, the NE breaks down and then reforms during cell division, and in interphase it is restored shortly after the NE rupture induced by mechanical force. In this way, the partitioning effect is regulated through dynamic processes throughout the cell cycle. A failure in rebuilding the NE structure triggers the mixing of nuclear and cytoplasmic contents, leading to catastrophic consequences for the nuclear functions. Whereas the precise details of molecular mechanisms for NE reformation during cell division and NE restoration in interphase are still being investigated, here, we mostly focus on mammalian cells to describe key aspects that have been identified and to discuss the crosstalk between them.</p>","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"15 1","pages":"2352203"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11123513/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141082964","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}
Nucleus (Austin, Tex.)Pub Date : 2024-12-01Epub Date: 2023-12-25DOI: 10.1080/19491034.2023.2296243
Huan-Lei Liu, Hao Nan, Wan-Wen Zhao, Xiang-Bo Wan, Xin-Juan Fan
{"title":"Phase separation in DNA double-strand break response.","authors":"Huan-Lei Liu, Hao Nan, Wan-Wen Zhao, Xiang-Bo Wan, Xin-Juan Fan","doi":"10.1080/19491034.2023.2296243","DOIUrl":"10.1080/19491034.2023.2296243","url":null,"abstract":"<p><p>DNA double-strand break (DSB) is the most dangerous type of DNA damage, which may lead to cell death or oncogenic mutations. Homologous recombination (HR) and nonhomologous end-joining (NHEJ) are two typical DSB repair mechanisms. Recently, many studies have revealed that liquid-liquid phase separation (LLPS) plays a pivotal role in DSB repair and response. Through LLPS, the crucial biomolecules are quickly recruited to damaged sites with a high concentration to ensure DNA repair is conducted quickly and efficiently, which facilitates DSB repair factors activating downstream proteins or transmitting signals. In addition, the dysregulation of the DSB repair factor's phase separation has been reported to promote the development of a variety of diseases. This review not only provides a comprehensive overview of the emerging roles of LLPS in the repair of DSB but also sheds light on the regulatory patterns of phase separation in relation to the DNA damage response (DDR).</p>","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"15 1","pages":"2296243"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10761171/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139038297","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}
Cinzia Klemm, Guðjón Ólafsson, Henry Richard Wood, Caitlin Mellor, Nicolae Radu Zabet, Peter Harold Thorpe
{"title":"Proteome-wide forced interactions reveal a functional map of cell-cycle phospho-regulation in <i>S. cerevisiae</i>.","authors":"Cinzia Klemm, Guðjón Ólafsson, Henry Richard Wood, Caitlin Mellor, Nicolae Radu Zabet, Peter Harold Thorpe","doi":"10.1080/19491034.2024.2420129","DOIUrl":"10.1080/19491034.2024.2420129","url":null,"abstract":"<p><p>Dynamic protein phosphorylation and dephosphorylation play an essential role in cell cycle progression. Kinases and phosphatases are generally highly conserved across eukaryotes, underlining their importance for post-translational regulation of substrate proteins. In recent years, advances in phospho-proteomics have shed light on protein phosphorylation dynamics throughout the cell cycle, and ongoing progress in bioinformatics has significantly improved annotation of specific phosphorylation events to a given kinase. However, the functional impact of individual phosphorylation events on cell cycle progression is often unclear. To address this question, we used the Synthetic Physical Interactions (SPI) method, which enables the systematic recruitment of phospho-regulators to most yeast proteins. Using this method, we identified several putative novel targets involved in chromosome segregation and cytokinesis. The SPI method monitors cell growth and, therefore, serves as a tool to determine the impact of protein phosphorylation on cell cycle progression.</p>","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"15 1","pages":"2420129"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11622623/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142775334","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}
Nucleus (Austin, Tex.)Pub Date : 2024-12-01Epub Date: 2024-01-27DOI: 10.1080/19491034.2024.2306777
Eugene V Makeyev, Sui Huang
{"title":"The perinucleolar compartment: structure, function, and utility in anti-cancer drug development.","authors":"Eugene V Makeyev, Sui Huang","doi":"10.1080/19491034.2024.2306777","DOIUrl":"10.1080/19491034.2024.2306777","url":null,"abstract":"<p><p>The perinucleolar compartment (PNC) was initially identified as a nuclear structure enriched for the polypyrimidine tract-binding protein. Since then, the PNC has been implicated in carcinogenesis. The prevalence of this compartment is positively correlated with disease progression in various types of cancer, and its expression in primary tumors is linked to worse patient outcomes. Using the PNC as a surrogate marker for anti-cancer drug efficacy has led to the development of a clinical candidate for anti-metastasis therapies. The PNC is a multicomponent nuclear body situated at the periphery of the nucleolus. Thus far, several non-coding RNAs and RNA-binding proteins have been identified as the PNC components. Here, we summarize the current understanding of the structure and function of the PNC, as well as its recurrent links to cancer progression and metastasis.</p>","PeriodicalId":74323,"journal":{"name":"Nucleus (Austin, Tex.)","volume":"15 1","pages":"2306777"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10824145/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139572253","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}