Journal ArticleDOI
Mechanisms and functions of nuclear envelope remodelling
Rosemarie Ungricht,Ulrike Kutay +1 more
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TLDR
The nuclear envelope is shown to be a dynamic and highly adaptable boundary that changes composition during differentiation, deforms in response to mechanical challenges, can be repaired upon rupture and even rapidly disassembles and reforms during open mitosis.Abstract:
As a compartment border, the nuclear envelope (NE) needs to serve as both a protective membrane shell for the genome and a versatile communication interface between the nucleus and the cytoplasm. Despite its important structural role in sheltering the genome, the NE is a dynamic and highly adaptable boundary that changes composition during differentiation, deforms in response to mechanical challenges, can be repaired upon rupture and even rapidly disassembles and reforms during open mitosis. NE remodelling is fundamentally involved in cell growth, division and differentiation, and if perturbed can lead to devastating diseases such as muscular dystrophies or premature ageing.read more
Citations
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Journal ArticleDOI
Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis
Bernhard Hampoelz,Andre Schwarz,Paolo Ronchi,Helena Bragulat-Teixidor,Christian Tischer,Imre Gaspar,Anne Ephrussi,Yannick Schwab,Martin Beck +8 more
TL;DR: It is shown that during Drosophila oogenesis, Nucleoporins condense into different precursor granules that interact and progress into NPCs, a non-canonical NPC assembly mechanism that relies on N nucleoporin condensates and occurs away from the nucleus under conditions of cell cycle arrest.
Journal ArticleDOI
Phosphatases in Mitosis: Roles and Regulation.
TL;DR: This review will focus on the established and emerging roles of mitotic phosphatases, describe their structural and biochemical properties, and discuss recent advances in understanding the regulation of phosphatase activity and function.
Journal ArticleDOI
Channel Nucleoporins Recruit PLK-1 to Nuclear Pore Complexes to Direct Nuclear Envelope Breakdown in C. elegans.
Lisa Martino,Stéphanie Morchoisne-Bolhy,Dhanya K. Cheerambathur,Lucie Van Hove,Julien Dumont,Nicolas Joly,Arshad Desai,Valérie Doye,Lionel Pintard +8 more
TL;DR: It is concluded that nucleoporins play an unanticipated regulatory role in NEBD, by recruiting PLK-1 to the NE thereby facilitating phosphorylation of critical downstream targets.
Journal ArticleDOI
Chromosome clustering by Ki-67 excludes cytoplasm during nuclear assembly
Sara Cuylen-Haering,Sara Cuylen-Haering,Mina Petrovic,Alberto Hernandez-Armendariz,Maximilian W. G. Schneider,Matthias Samwer,Claudia Blaukopf,Liam J. Holt,Daniel W. Gerlich +8 more
TL;DR: The study reveals that chromosome mechanics help to re-establish the compartmentalization of eukaryotic cells after open mitosis and shows that the exclusion of mature ribosomes from the nucleus after mitosis depends on Ki-67-regulated chromosome clustering.
Posted ContentDOI
Nuclear envelope assembly defects link mitotic errors to chromothripsis
TL;DR: These findings indicate that chromosome segregation and NE assembly are only loosely coordinated through the timing of mitotic spindle disassembly, and that micronuclei have impaired nuclear import, and key nuclear proteins required to maintain the integrity of the NE and the genome fail to accumulate normally.
References
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Journal ArticleDOI
Massive Genomic Rearrangement Acquired in a Single Catastrophic Event during Cancer Development
Philip J. Stephens,Christopher Greenman,Beiyuan Fu,Fengtang Yang,Graham R. Bignell,Laura Mudie,Erin Pleasance,King Wai Lau,David Beare,Lucy Stebbings,Stuart McLaren,Meng-Lay Lin,David J. McBride,Ignacio Varela,Serena Nik-Zainal,Catherine Leroy,Mingming Jia,Andrew Menzies,Adam Butler,Jon W. Teague,Michael A. Quail,John Burton,Harold Swerdlow,Nigel P. Carter,Laura Morsberger,Christine A. Iacobuzio-Donahue,George A. Follows,Anthony R. Green,Adrienne M. Flanagan,Adrienne M. Flanagan,Michael R. Stratton,P. Andrew Futreal,Peter J. Campbell,Peter J. Campbell +33 more
TL;DR: It is found that one, or indeed more than one, cancer-causing lesion can emerge out of the genomic crisis, which has important implications for the origins of genomic remodeling and temporal emergence of cancer.
Journal ArticleDOI
Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome
Maria Eriksson,W. Ted Brown,Leslie B. Gordon,Leslie B. Gordon,Michael W. Glynn,Joel Singer,Laura J. Scott,Michael R. Erdos,Christiane M. Robbins,Tracy Moses,Peter Berglund,Amalia Dutra,Evgenia Pak,Sandra G. Durkin,Antonei B. Csoka,Michael Boehnke,Thomas W. Glover,Francis S. Collins +17 more
TL;DR: Evidence of mutations in lamin A (LMNA) as the cause of Hutchinson–Gilford progeria syndrome is presented, and the discovery of the molecular basis of this disease may shed light on the general phenomenon of human ageing.
Journal ArticleDOI
Domain organization of human chromosomes revealed by mapping of nuclear lamina interactions
Lars Guelen,Ludo Pagie,Emilie Brasset,Wouter Meuleman,Wouter Meuleman,Marius B. Faza,Wendy Talhout,Bert H.J. Eussen,Annelies de Klein,Lodewyk F. A. Wessels,Lodewyk F. A. Wessels,Wouter de Laat,Bas van Steensel +12 more
TL;DR: A high-resolution map of the interaction sites of the entire genome with NL components in human fibroblasts is constructed and demonstrates that the human genome is divided into large, discrete domains that are units of chromosome organization within the nucleus.
Journal ArticleDOI
Nuclear lamin-A Scales With Tissue Stiffness and Enhances Matrix-Directed Differentiation
Joe Swift,Irena L. Ivanovska,Amnon Buxboim,Takamasa Harada,P.C. Dave P. Dingal,Joel Pinter,J. David Pajerowski,Kyle R. Spinler,Jae-Won Shin,Manorama Tewari,Florian Rehfeldt,David W. Speicher,Dennis E. Discher,Dennis E. Discher +13 more
TL;DR: In this article, proteomics analyses revealed that levels of the nucleoskeletal protein lamin-A scaled with tissue elasticity, as did levels of collagens in the extracellular matrix that determine E.
Journal ArticleDOI
Genomic Instability and Aging-like Phenotype in the Absence of Mammalian SIRT6
Raul Mostoslavsky,Katrin F. Chua,Katrin F. Chua,David B. Lombard,Wendy W. Pang,Miriam R. Fischer,Lionel Gellon,Pingfang Liu,Gustavo Mostoslavsky,Sonia Franco,Michael M. Murphy,Kevin D. Mills,Parin Patel,Joyce T. Hsu,Andrew L. Hong,Ethan Ford,Hwei Ling Cheng,Caitlin Kennedy,Nomeli P. Nunez,Nomeli P. Nunez,Roderick T. Bronson,David Frendewey,Wojtek Auerbach,David M. Valenzuela,Margaret Karow,Michael O. Hottiger,Stephen D. Hursting,J. Carl Barrett,J. Carl Barrett,Leonard Guarente,Richard C. Mulligan,Bruce Demple,George D. Yancopoulos,Frederick W. Alt +33 more
TL;DR: It is demonstrated that SIRT6 is a nuclear, chromatin-associated protein that promotes resistance to DNA damage and suppresses genomic instability in mouse cells, in association with a role in base excision repair (BER).