Relevant bibliographies by topics / Cell migration Nuclear envelope

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Cell migration Nuclear envelope'

Author: Grafiati
Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Cell migration Nuclear envelope"

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Bone, Courtney R., Erin C. Tapley, Mátyás Gorjánácz, and Daniel A. Starr. "The Caenorhabditis elegans SUN protein UNC-84 interacts with lamin to transfer forces from the cytoplasm to the nucleoskeleton during nuclear migration." Molecular Biology of the Cell 25, no. 18 (September 15, 2014): 2853–65. http://dx.doi.org/10.1091/mbc.e14-05-0971.

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Nuclear migration is a critical component of many cellular and developmental processes. The nuclear envelope forms a barrier between the cytoplasm, where mechanical forces are generated, and the nucleoskeleton. The LINC complex consists of KASH proteins in the outer nuclear membrane and SUN proteins in the inner nuclear membrane that bridge the nuclear envelope. How forces are transferred from the LINC complex to the nucleoskeleton is poorly understood. The Caenorhabditis elegans lamin, LMN-1, is required for nuclear migration and interacts with the nucleoplasmic domain of the SUN protein UNC-84. This interaction is weakened by the unc-84(P91S) missense mutation. These mutant nuclei have an intermediate nuclear migration defect—live imaging of nuclei or LMN-1::GFP shows that many nuclei migrate normally, others initiate migration before subsequently failing, and others fail to begin migration. At least one other component of the nucleoskeleton, the NET5/Samp1/Ima1 homologue SAMP-1, plays a role in nuclear migration. We propose a nut-and-bolt model to explain how forces are dissipated across the nuclear envelope during nuclear migration. In this model, SUN/KASH bridges serve as bolts through the nuclear envelope, and nucleoskeleton components LMN-1 and SAMP-1 act as both nuts and washers on the inside of the nucleus.
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Denais, C. M., R. M. Gilbert, P. Isermann, A. L. McGregor, M. te Lindert, B. Weigelin, P. M. Davidson, P. Friedl, K. Wolf, and J. Lammerding. "Nuclear envelope rupture and repair during cancer cell migration." Science 352, no. 6283 (March 24, 2016): 353–58. http://dx.doi.org/10.1126/science.aad7297.

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Fridolfsson, Heidi N., and Daniel A. Starr. "Kinesin-1 and dynein at the nuclear envelope mediate the bidirectional migrations of nuclei." Journal of Cell Biology 191, no. 1 (October 4, 2010): 115–28. http://dx.doi.org/10.1083/jcb.201004118.

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Kinesin-1 and dynein are recruited to the nuclear envelope by the Caenorhabditis elegans klarsicht/ANC-1/Syne homology (KASH) protein UNC-83 to move nuclei. The mechanisms of how these motors are coordinated to mediate nuclear migration are unknown. Time-lapse differential interference contrast and fluorescence imaging of embryonic hypodermal nuclear migration events were used to characterize the kinetics of nuclear migration and determine microtubule dynamics and polarity. Wild-type nuclei display bidirectional movements during migration and are also able to roll past cytoplasmic granules. unc-83, unc-84, and kinesin-1 mutants have severe nuclear migration defects. Without dynein, nuclear migration initiates normally but lacks bidirectional movement and shows defects in nuclear rolling, implicating dynein in resolution of cytoplasmic roadblocks. Microtubules are highly dynamic during nuclear migration. EB1::green fluorescence protein imaging demonstrates that microtubules are polarized in the direction of nuclear migration. This organization of microtubules fits with our model that kinesin-1 moves nuclei forward and dynein functions to move nuclei backward for short stretches to bypass cellular roadblocks.
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McGee, Matthew D., Regina Rillo, Amy S. Anderson, and Daniel A. Starr. "UNC-83 Is a KASH Protein Required for Nuclear Migration and Is Recruited to the Outer Nuclear Membrane by a Physical Interaction with the SUN Protein UNC-84." Molecular Biology of the Cell 17, no. 4 (April 2006): 1790–801. http://dx.doi.org/10.1091/mbc.e05-09-0894.

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UNC-84 is required to localize UNC-83 to the nuclear envelope where it functions during nuclear migration. A KASH domain in UNC-83 was identified. KASH domains are conserved in the nuclear envelope proteins Syne/nesprins, Klarsicht, MSP-300, and ANC-1. Caenorhabditis elegans UNC-83 was shown to localize to the outer nuclear membrane and UNC-84 to the inner nuclear membrane in transfected mammalian cells, suggesting the KASH and SUN protein targeting mechanisms are conserved. Deletion of the KASH domain of UNC-83 blocked nuclear migration and localization to the C. elegans nuclear envelope. Some point mutations in the UNC-83 KASH domain disrupted nuclear migration, even if they localized normally. At least two separable portions of the C-terminal half of UNC-84 were found to interact with the UNC-83 KASH domain in a membrane-bound, split-ubiquitin yeast two-hybrid system. However, the SUN domain was essential for UNC-84 function and UNC-83 localization in vivo. These data support the model that KASH and SUN proteins bridge the nuclear envelope, connecting the nuclear lamina to cytoskeletal components. This mechanism seems conserved across eukaryotes and is the first proposed mechanism to target proteins specifically to the outer nuclear membrane.
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Alvarado-Kristensson, Maria, and Catalina Ana Rosselló. "The Biology of the Nuclear Envelope and Its Implications in Cancer Biology." International Journal of Molecular Sciences 20, no. 10 (May 27, 2019): 2586. http://dx.doi.org/10.3390/ijms20102586.

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The formation of the nuclear envelope and the subsequent compartmentalization of the genome is a defining feature of eukaryotes. Traditionally, the nuclear envelope was purely viewed as a physical barrier to preserve genetic material in eukaryotic cells. However, in the last few decades, it has been revealed to be a critical cellular component in controlling gene expression and has been implicated in several human diseases. In cancer, the relevance of the cell nucleus was first reported in the mid-1800s when an altered nuclear morphology was observed in tumor cells. This review aims to give a current and comprehensive view of the role of the nuclear envelope on cancer first by recapitulating the changes of the nuclear envelope during cell division, second, by reviewing the role of the nuclear envelope in cell cycle regulation, signaling, and the regulation of the genome, and finally, by addressing the nuclear envelope link to cell migration and metastasis and its use in cancer prognosis.
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Ha, Mihyang, Ji-Young Kim, Myoung-Eun Han, Ga Hyun Kim, Si Young Park, Dae Cheon Jeong, Sae-Ock Oh, and Yun Hak Kim. "TMEM18: A Novel Prognostic Marker in Acute Myeloid Leukemia." Acta Haematologica 140, no. 2 (2018): 71–76. http://dx.doi.org/10.1159/000492742.

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Background: Certain nuclear envelope proteins are associated with important cancer cell characteristics, including migration and proliferation. Abnormal expression of and genetic changes in nuclear envelope proteins have been reported in acute myeloid leukemia (AML) patients. Transmembrane protein 18 (TMEM18), a nuclear envelope protein, is involved in neural stem cell migration and tumorigenicity. Methods: To examine the prognostic significance of TMEM18 in AML patients, we analyzed an AML cohort from The Cancer Genome Atlas (TCGA, n = 142). Results: Kaplan-Meier survival analysis revealed that TMEM18 overexpression was associated with a better AML prognosis with good discrimination (p = 0.019). Interestingly, this ability to predict the prognosis was significant in male AML patients, but not in female ones. C-index and area-under-the-curve analyses further supported this discriminative ability and multivariate analysis confirmed its prognostic significance (p = 0.00347). Correlation analysis revealed that TMEM18 had a statistically significant positive correlation with nuclear envelop protein 133 (NUP133), NUP35, NUP54, NUP62, and NUP88. Conclusion: Because the current AML prognostic factors do not take mRNA expression into consideration unlike other cancers, the development of mRNA-based prognostic factors would be beneficial for accurate prediction of the survival of AML patients. Therefore, TMEM18 gene is a potential biomarker for AML.
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Saunders, Cosmo A., Nathan J. Harris, Patrick T. Willey, Brian M. Woolums, Yuexia Wang, Alex J. McQuown, Amy Schoenhofen, et al. "TorsinA controls TAN line assembly and the retrograde flow of dorsal perinuclear actin cables during rearward nuclear movement." Journal of Cell Biology 216, no. 3 (February 27, 2017): 657–74. http://dx.doi.org/10.1083/jcb.201507113.

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The nucleus is positioned toward the rear of most migratory cells. In fibroblasts and myoblasts polarizing for migration, retrograde actin flow moves the nucleus rearward, resulting in the orientation of the centrosome in the direction of migration. In this study, we report that the nuclear envelope–localized AAA+ (ATPase associated with various cellular activities) torsinA (TA) and its activator, the inner nuclear membrane protein lamina-associated polypeptide 1 (LAP1), are required for rearward nuclear movement during centrosome orientation in migrating fibroblasts. Both TA and LAP1 contributed to the assembly of transmembrane actin-associated nuclear (TAN) lines, which couple the nucleus to dorsal perinuclear actin cables undergoing retrograde flow. In addition, TA localized to TAN lines and was necessary for the proper mobility of EGFP-mini–nesprin-2G, a functional TAN line reporter construct, within the nuclear envelope. Furthermore, TA and LAP1 were indispensable for the retrograde flow of dorsal perinuclear actin cables, supporting the recently proposed function for the nucleus in spatially organizing actin flow and cytoplasmic polarity. Collectively, these results identify TA as a key regulator of actin-dependent rearward nuclear movement during centrosome orientation.
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Dufresne, L., I. Neant, J. St-Pierre, F. Dube, and P. Guerrier. "Effects of 6-dimethylaminopurine on microtubules and putative intermediate filaments in sea urchin embryos." Journal of Cell Science 99, no. 4 (August 1, 1991): 721–30. http://dx.doi.org/10.1242/jcs.99.4.721.

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The effects of 6-dimethylaminopurine (6-DMAP) (a putative phosphorylation inhibitor) on the state of assembly of microtubules and intermediate filaments have been studied during the first cell cycle of the sea urchin Strongylocentrotus droebachiensis. Changes in the spatial organization of cytoskeletal structures were studied by indirect immunofluorescence with anti-tubulin and anti-IFa antibodies. The rates and patterns of protein phosphorylation in control and treated eggs were also investigated. The transfer of fertilized eggs to 600 microM 6-DMAP within 4 min following insemination inhibits pronuclear migration and syngamy. This also prevents male pronuclear decondensation, while chromatin condensation and nuclear envelope breakdown do not occur in the female pronucleus. Immunolabeling with anti-tubulin antibodies reveals the presence of cortical microtubules as early as 15 min after fertilization in both control and treated eggs. However, no sperm astral microtubules could be detected in the treated eggs. At later stages, from syngamy (40 min) up to nuclear envelope breakdown (90 min), 6-DMAP affects neither cortical microtubule organization nor the state of chromatin condensation but it precludes nuclear envelope breakdown and entry into mitosis. Treatment of the fertilized eggs after nuclear envelope breakdown induces permanent chromosome decondensation and premature disappearance of the mitotic apparatus. This last event involves disruption of the spatial organization of both microtubules and putative intermediate filaments. Quantitative measurements of protein phosphorylation show that 6-DMAP efficiently and reversibly inhibits 32P incorporation into proteins. Qualitative analysis of the autoradiograms of 32P-labeled proteins separated by SDS-PAGE reveals that a major protein band, migrating with an apparent molecular weight of 31 × 10(3)Mr, is specifically dephosphorylated in eggs treated with 6-DMAP. This study suggests that protein phosphorylation is required for sperm aster microtubule growth and migration, but not for cortical microtubule polymerization. It also strengthens the hypothesis that, in sea urchin eggs, putative intermediate filaments are tightly associated with spindle microtubules. Finally, it confirms that inhibiting protein phosphorylation before nuclear envelope breakdown reversibly prevents the entry into mitosis.
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Islam, Md Ariful, Ho Jin Choi, Raju Dash, Syeda Ridita Sharif, Diyah Fatimah Oktaviani, Dae-Hyun Seog, and Il Soo Moon. "N-Acetyl-d-Glucosamine Kinase Interacts with NudC and Lis1 in Dynein Motor Complex and Promotes Cell Migration." International Journal of Molecular Sciences 22, no. 1 (December 24, 2020): 129. http://dx.doi.org/10.3390/ijms22010129.

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Recently, we showed that N-acetylglucosamine kinase (NAGK), an enzyme of amino sugar metabolism, interacts with dynein light chain roadblock type 1 (DYNLRB1) and promotes the functions of dynein motor. Here, we report that NAGK interacts with nuclear distribution protein C (NudC) and lissencephaly 1 (Lis1) in the dynein complex. Yeast two-hybrid assays, pull-down assays, immunocytochemistry, and proximity ligation assays revealed NAGK–NudC–Lis1–dynein complexes around nuclei, at the leading poles of migrating HEK293T cells, and at the tips of migratory processes of cultured rat neuroblast cells. The exogenous expression of red fluorescent protein (RFP)-tagged NAGK accelerated HEK293T cell migration during in vitro wound-healing assays and of neurons during in vitro neurosphere migration and in utero electroporation assays, whereas NAGK knockdown by short hairpin RNA (shRNA) delayed migration. Finally, a small NAGK peptide derived from the NudC interacting domain in in silico molecular docking analysis retarded the migrations of HEK293T and SH-SY5Y cells. These data indicate a functional interaction between NAGK and dynein–NudC–Lis1 complex at the nuclear envelope is required for the regulation of cell migration.
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Lee, Kenneth K., Daniel Starr, Merav Cohen, Jun Liu, Min Han, Katherine L. Wilson, and Yosef Gruenbaum. "Lamin-dependent Localization of UNC-84, A Protein Required for Nuclear Migration in Caenorhabditis elegans." Molecular Biology of the Cell 13, no. 3 (March 2002): 892–901. http://dx.doi.org/10.1091/mbc.01-06-0294.

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Mutations in the Caenorhabditis elegans unc-84 gene cause defects in nuclear migration and anchoring. We show that endogenous UNC-84 protein colocalizes with Ce-lamin at the nuclear envelope and that the envelope localization of UNC-84 requires Ce-lamin. We also show that during mitosis, UNC-84 remains at the nuclear periphery until late anaphase, similar to known inner nuclear membrane proteins. UNC-84 protein is first detected at the 26-cell stage and thereafter is present in most cells during development and in adults. UNC-84 is properly expressed in unc-83 andanc-1 lines, which have phenotypes similar tounc-84, suggesting that neither the expression nor nuclear envelope localization of UNC-84 depends on UNC-83 or ANC-1 proteins. The envelope localization of Ce-lamin, Ce-emerin, Ce-MAN1, and nucleoporins are unaffected by the loss of UNC-84. UNC-84 is not required for centrosome attachment to the nucleus because centrosomes are localized normally in unc-84 hyp7 cells despite a nuclear migration defect. Models for UNC-84 localization are discussed.
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Dissertations / Theses on the topic "Cell migration Nuclear envelope"

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KIDIYOOR, GURURAJ RAO. "ATR MEDIATED REGULATION OF CELLULAR AND NUCLEAR PLASTICITY." Doctoral thesis, Università degli Studi di Milano, 2018. http://hdl.handle.net/2434/561090.

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Protein kinase ATR (Ataxia Telangiectasia and Rad3-related) is a key regulator of genomic integrity. In addition to its vital, well-understood role in maintaining replication fork stability, ATR is also involved in mediating mechanical stress response at the nuclear envelope preventing potential threats to the genome. Our data from sub-cellular distribution and interactome analysis of ATR suggests that ATR contributes to several cellular processes in multiple organelles such as mitochondria, actin cytoskeleton, Golgi and nuclear envelope. At the nuclear envelope ATR is present on both inner and outer nuclear membranes, on the nuclear pores and bound to perinuclear chromatin and to perinuclear actin fibers. In this study we show that ATR regulates nuclear membrane integrity by maintaining nuclear morphology and optimal membrane tension, by counteracting mechanical force imbalances at the NE and by coordinating nuclear events with nuclear and cell migration. We report a novel role of ATR in preventing and protecting nuclear envelope damage and DNA damage caused by mechanical constrains acting on the nucleus. Further we show that by maintaining nuclear envelope integrity ATR facilitates cell migration on 2D surfaces and by regulating nuclear membrane components and by limiting nuclear envelope damage it aids cell survival during confined 3D migrations. Loss of ATR dampens neuronal migration during development and cancer cells lacking ATR are inefficient in extravasation, do not survive circulation and fail to successfully metastasize into the host environment. Therefore, by promoting cell survival in altering mechanical microenvironment and during metastasis and invasion, ATR assists tumor development, suggesting a dual role for this kinase in tumorigenisis
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Jaffer, Ali Mohammed Hakim. "Multifaceted roles of the transmembrane nuclear envelope protein, Samp1." Doctoral thesis, Stockholms universitet, Institutionen för neurokemi, 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-141816.

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The eukaryotic nuclear envelope (NE), separates the nucleoplasm from cytoplasm and is made up of two concentric lipid membranes, the outer and the inner nuclear membranes (ONM and INM), the nuclear pore complexes (NPCs) and an underlying filamentous nuclear lamina. The INM contains hundreds of unique transmembrane proteins of which only a handful have been characterized. In this thesis, I aimed to understand the functional organization of proteins in the nuclear envelope and I focused on investigating the functions of a recently identified INM transmembrane protein, Samp1. We have developed a novel and robust approach, MCLIP, to identify specific protein-protein interactions taking place in live cells. Using MCLIP, we have shown that Samp1 interacts with proteins of the LINC complex, the nuclear lamina and components of the mitotic spindle. Samp1's specific interactions with a variety of binding partners, suggest that Samp1 plays important roles both in interphase and in mitosis.  We have also shown that Samp1 can provide a binding site at the INM for the GTPase Ran, a master regulator of protein interactions in interphase and in mitosis. Furthermore, we have also investigated the role of Samp1 in cell differentiation using two independent model systems. In human iPSCs, ectopic expression of Samp1 promoted differentiation despite pluripotent culture conditions. In C2C12 myoblast, depletion of Samp1 completely blocked differentiation into myotubes. The two studies complement each other and suggest that Samp1 has a strong differentiation promoting activity. Taken together, the findings in this thesis, give insights on the unexpected and unforeseen roles played by a transmembrane protein in different fundamental cellular process.

At the time of the doctoral defense, the following papers were unpublished and had a status as follows: Paper 3: Manuscript. Paper 4: Manuscript. Paper 5: Manuscript.

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Sabbatini, G. P., and G. P. Sabbatini. "Rat liver nuclear envelope insulin binding and its effects on endogenous protein kinases." Doctoral thesis, University of Cape Town, 1992. http://hdl.handle.net/11427/23361.

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The postulated model for the insulin - stimulated induction of mRNA efflux (Purrello et al., 1983) is based on the demonstrated binding of insulin to intracellular membrane structures (see chapter 2, section 2.2.1), and the in vitro effect of insulin on nuclear envelope phosphorylation, NTPase activity, and mRNA efflux (see chapter 5, section 5.1). These independent observations have led to the development of a model for the direct induction by insulin, at the level of the nucleus, of mRNA efflux (figure 1.1). However, the specific intracellular insulin binding has been inf erred from kinetic or morphological studies which have not identified a discrete membrane - bound polypeptide(s) as an insulin docking molecule in situ (Goldfine, 1981). Also, the stimulation of NTPase activity has only been established by monitoring the level of general ATP hydrolysis of nuclear envelope fractions in the presence and absence of insulin (Purrello et al., 1983). The scope of this thesis has been to further the understanding of this mechanism by attempting to a) unequivocally identify a specific nuclear envelope - associated insulin docking polypeptide in situ and b) to demonstrate that insulin directly affects the ATP - binding of nuclear envelope ATP - binding proteins. The latter would demonstrate a primary effect of insulin i.e. the modulation of the ATP - binding capacity of identified NTPases / protein kinases (or their release from some inactive storage form), and not a general phenomenon such as elevated ATP.
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Bermeo, Serrato Sandra Milena. "Role of the Proteins of the Nuclear Envelope in Mesenchymal Stem Cell Differentiation." Thesis, The University of Sydney, 2015. http://hdl.handle.net/2123/14373.

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The nuclear envelope (NE) provides stiffness to the nucleus, protects the genome, and regulates the mechanotransduction process via its network of proteins. These roles govern gene transcription and cell survival and/or differentiation. Considering that these proteins transmit cytoplasmic signalling to the nucleus through interactions with transcription factors, the identification and control of these interactions could play an important role in the regulation of cell differentiation and survival. In mesenchymal stem cells (MSCs), it has been demonstrated that NE proteins are crucial to the differentiation process. Mutations in some of them are linked to envelopathies, in which mesenchymal tissues are differentially affected. In addition, during the ageing process, their level is decreased, which would explain in part some of the age-related changes in bone and muscle. Lamin A, emerin and MAN1 are the most studied NE proteins in terms of their involvement in the pathogenesis of envelopathies. In this thesis we hypothesized that these NE proteins are involved in the differentiation of MSCs into bone and fat, playing a role in the pathogenesis of age-related bone loss. Therefore, this research thesis reports new evidence on the role of these three proteins during osteoblastic and adipogenic differentiation of bone marrow-derived human MSCs.
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BERTORA, STEFANIA. "ROLE OF NUCLEAR ENVELOPE PROTEIN MAN1 IN NUCLEAR ORGANISATION AND MAINTENANCE OF GENOME STABILITY." Doctoral thesis, Università degli Studi di Milano, 2018. http://hdl.handle.net/2434/554706.

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The eukaryotic cell nucleus is characterized by a defined spatial organization of the chromatin, which relies on the physical tethering of many genomic loci to the inner surface of the nuclear envelope. This interaction is mainly mediated by lamins and lamin-associated proteins, which create a protein network at the nuclear periphery called nuclear lamina. Man1 is a member of a lamin-associated protein family known as LEM-domain proteins, which are characterized by the presence of a highly conserved domain, called LEM, that mediates the interaction with the chromatin. Data obtained with the yeast Man1 homolog Src1 underline the importance of this protein in different processes of the cell cycle, such as chromosome segregation, nuclear pores assembly, gene expression, chromatin organization and maintenance of genome stability, while in animal models, the function of Man1 has been associated to the regulation of developmental signalling pathways during embryogenesis. In this study, truncated recombinant mutants of Man1, containing the LEM domain, were shown to inhibit nuclear assembly and alter nuclear pore formation when added to Xenopus laevis cell-free extracts. Moreover, Xenopus nuclei assembled in the presence of Man1 truncated fragments were characterized by defects in chromatin organization, DNA replication and accumulation of DNA damage and, as a consequence, they failed to progress through mitosis. Furthermore, mouse embryonic stem cells (mESCs) depleted for Man1 showed evident signs of spontaneous differentiation, indicating inability in the maintenance of stem cell features. Intriguingly, preliminary analysis of Man1-knockout mESCs transcriptional profile showed an alteration of gene expression at the level of pericentromeric and telomeric regions, underlining a potential link between Man1 and genomic stability of these particular regions. In conclusion, this study illustrates the importance of Man1 in ensuring the proper chromatin organization necessary to support different cellular and DNA metabolic processes.
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Anna, Newman-Griffis Hare. "Plant nuclear envelope-associated proteins function in development and symbiosis." The Ohio State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=osu1542733901078983.

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Hattier, Thomas. "Investigation of Laminopathy-Like Alterations of the Nuclear Envelope caused by Accumulation of Esc1p." Case Western Reserve University School of Graduate Studies / OhioLINK, 2006. http://rave.ohiolink.edu/etdc/view?acc_num=case1138383986.

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Chemudupati, Mahesh. "Investigating the effects of nuclear envelope proteins on nuclear structure and organization in Aspergillus nidulans." The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu148009978216118.

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Wylde, George William. "Mechanotransduction at the nuclear envelope : the role of forces in facilitating embryonic stem cell fate decisions." Thesis, University of Cambridge, 2017. https://www.repository.cam.ac.uk/handle/1810/267909.

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While a large body of work has focused on the transcriptional regulation of cellular identity, the role of the mechanical properties of cells and the importance of their physical interactions with the local environment remains less well understood. In this project, we explored the impact of cytoskeleton-generated forces exerted on the nucleus in the context of early embryonic stem (ES) cell fate decisions. We chose to perturb force generating components in the cytoskeleton – notably the molecular motor non-muscle myosin II - and key structural and chromatin binding proteins in the nuclear envelope, notably, the lamins (LMNA), Lamin B receptor (LBR) and components of the LINC complex (nesprins/KASH). The structural proteins in the nuclear envelope regulate both the mechanical response of the nucleus to force and the stabilization of peripheral heterochromatin (repressed genes). Our hypothesis is that reducing forces transmitted directly to chromatin or increasing tethering of peripheral heterochromatin to the nuclear envelope would restrict access to lineage specific genes sequestered at the nuclear lamina and thereby either impair, or delay, differentiation. We found phenotypes in the capacity of mouse ES cells to specify to the neural lineage following our perturbations: overexpression of LMNA, LBR and KASH proteins resulted in a significant fraction of cells that did not express the neuroectoderm marker Sox1 after four days of differentiation, while inhibiting non-muscle myosin II delayed Sox1 expression in the entire population. Overexpression of LMNA and LBR did not affect the ability of the cells to exit the naive pluripotent state, which raises the possibility that the perturbations are halting the cells in a formative phase prior to lineage specification. Future work will focus on looking at genome-wide transcriptional changes accompanying differentiation combined with an analysis of spatial information of differentially regulated genes.
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Vollmar, Friederike Lara Veronika. "Analyse der Kernhüllenbildung am Modellsystem Xenopus laevis = Studying nuclear envelope assembly in the cell-free system derived from Xenopus laevis eggs." kostenfrei, 2008. http://www.opus-bayern.de/uni-wuerzburg/volltexte/2009/2929/.

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Books on the topic "Cell migration Nuclear envelope"

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Reipert, Siegfried. Structural characterisation of the nuclear envelope during the cell cycle: A methodological approach. Manchester: University of Manchester, 1993.

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Collas, Philippe, Sue Shackleton, and Eric C. Schirmer. Nuclear Envelope: Methods and Protocols. Springer New York, 2018.

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Collas, Philippe, Sue Shackleton, and Eric C. Schirmer. The Nuclear Envelope: Methods and Protocols. Humana, 2016.

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Nuclear Transport (Results and Problems in Cell Differentiation). Springer, 2001.

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Oakford, Lawrence Xavier. The isolation and initial characterization of nuclear envelope "ghosts" and nuclear pore complex morphology from Physarum polycephalum. 1986.

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Schirmer, Eric C., and Jose I. de las Heras. Cancer Biology and the Nuclear Envelope: Recent Advances May Elucidate Past Paradoxes. Springer, 2016.

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Schirmer, Eric C., and Jose I. de las Heras. Cancer Biology and the Nuclear Envelope: Recent Advances May Elucidate Past Paradoxes. Springer London, Limited, 2014.

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Schirmer, Eric C., and Jose I. de las Heras. Cancer Biology and the Nuclear Envelope: Recent Advances May Elucidate Past Paradoxes. Springer, 2014.

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Nuclear Organization in Development and Disease: Novartis Foundation Symposium (Novartis Foundation Symposia). Wiley, 2005.

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Book chapters on the topic "Cell migration Nuclear envelope"

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Svoren, Martin, Elena Camerini, Merijn van Erp, Feng Wei Yang, Gert-Jan Bakker, and Katarina Wolf. "Approaches to Determine Nuclear Shape in Cells During Migration Through Collagen Matrices." In Cell Migration in Three Dimensions, 97–114. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2887-4_7.

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AbstractFibrillar collagen is an abundant extracellular matrix (ECM) component of interstitial tissues which supports the structure of many organs, including the skin and breast. Many different physiological processes, but also pathological processes such as metastatic cancer invasion, involve interstitial cell migration. Often, cell movement takes place through small ECM gaps and pores and depends upon the ability of the cell and its stiff nucleus to deform. Such nuclear deformation during cell migration may impact nuclear integrity, such as of chromatin or the nuclear envelope, and therefore the morphometric analysis of nuclear shapes can provide valuable insight into a broad variety of biological processes. Here, we describe a protocol on how to generate a cell-collagen model in vitro and how to use confocal microscopy for the static and dynamic visualization of labeled nuclei in single migratory cells. We developed, and here provide, two scripts that (Fidler, Nat Rev Cancer 3(6):453–458, 2003) enable the semi-automated and fast quantification of static single nuclear shape descriptors, such as aspect ratio or circularity, and the nuclear irregularity index that forms a combination of four distinct shape descriptors, as well as (Frantz et al., J Cell Sci 123 (Pt 24):4195–4200, 2010) a quantification of their changes over time. Finally, we provide quantitative measurements on nuclear shapes from cells that migrated through collagen either in the presence or the absence of an inhibitor of collagen degradation, showing the distinctive power of this approach. This pipeline can also be applied to cell migration studied in different assays, ranging from 3D microfluidics to migration in the living organism.
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Razafsky, David, Denis Wirtz, and Didier Hodzic. "Nuclear Envelope in Nuclear Positioning and Cell Migration." In Cancer Biology and the Nuclear Envelope, 471–90. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4899-8032-8_21.

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Neumann, Sascha, and Angelika A. Noegel. "Nesprins in Cell Stability and Migration." In Cancer Biology and the Nuclear Envelope, 491–504. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4899-8032-8_22.

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Osorio, Daniel S., and Edgar R. Gomes. "Connecting the Nucleus to the Cytoskeleton for Nuclear Positioning and Cell Migration." In Cancer Biology and the Nuclear Envelope, 505–20. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4899-8032-8_23.

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Rose, Annkatrin. "Open Mitosis: Nuclear Envelope Dynamics." In Plant Cell Monographs, 207–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/7089_2007_128.

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Robson, Michael I., Phu Le Thanh, and Eric C. Schirmer. "NETs and Cell Cycle Regulation." In Cancer Biology and the Nuclear Envelope, 165–85. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4899-8032-8_8.

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Kennedy, Brian K., and Juniper K. Pennypacker. "RB and Lamins in Cell Cycle Regulation and Aging." In Cancer Biology and the Nuclear Envelope, 127–42. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4899-8032-8_6.

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Shimi, Takeshi, and Robert D. Goldman. "Nuclear Lamins and Oxidative Stress in Cell Proliferation and Longevity." In Cancer Biology and the Nuclear Envelope, 415–30. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4899-8032-8_19.

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Fragoso-Luna, Adrián, and Peter Askjaer. "The Nuclear Envelope in Ageing and Progeria." In Biochemistry and Cell Biology of Ageing: Part III Biomedical Science, 53–75. Cham: Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-21410-3_3.

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Pfeifer, Charlotte R., Jerome Irianto, and Dennis E. Discher. "Nuclear Mechanics and Cancer Cell Migration." In Advances in Experimental Medicine and Biology, 117–30. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-17593-1_8.

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Conference papers on the topic "Cell migration Nuclear envelope"

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Goto, Chieko. "The nuclear envelope protein KAKU4 affects the migration order of the vegetative nucleus and sperm cells in pollen tubes." In ASPB PLANT BIOLOGY 2020. USA: ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1052951.

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Gao, Jianjun, Xinbo Xu, and Fulin Su. "Range cell migration of SAR moving target based on envelope correlation method." In 2017 First International Conference on Electronics Instrumentation & Information Systems (EIIS). IEEE, 2017. http://dx.doi.org/10.1109/eiis.2017.8298558.

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Fan, Chunling, Zongming Fu, Qingning Su, Daniel J. Angelini, Jennifer Van Eyk, and Roger A. Johns. "S100A11 Mediates HIMF-induced Smooth Muscle Cell Migration, Vesicular Exocytosis And Nuclear Activation." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a6331.

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Hale, Tracy K., Sarah Bond, and David Wheeler. "Abstract 1887: Untethering heterochromatin: how loss of HP1a enhances cell invasion by altering nuclear envelope integrity." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-1887.

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McGregor, Alexandra L., Joshua J. Elacqua, Emily S. Bell, and Jan Lammerding. "Abstract 1897: The role of nuclear deformation and rupture in breast cancer cell migration." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-1897.

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Pidaparti, R. M., P. A. Sarma, A. S. C. Sinha, G. Vemuri, and A. M. Gacy. "Nuclear Membrane Dynamics of a Nuclear Pore Complex Structure." In ASME 2001 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2001. http://dx.doi.org/10.1115/imece2001/bed-23162.

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Abstract The nuclear pore complex (NPC) is an excellent example of a bio-molecular motor, since it operates primarily via energy dependent processes, and performs some of the most vital functions required for the survival of a cell. In the presence of appropriate chemical stimuli, the NPC apparently opens or closes, like a gating mechanism, and permits the flow of material in to and out of the nucleus. An NPC, with typical dimensions of 100–200 nm, is a megadalton (MDa) heteromultimeric protein complex, which spans the nuclear envelope and is postulated to possess a transporter-containing central cylindrical body embedded between cytoplasmic and nucleoplasmic rings as shown in Fig.1. A cell has many, presumably identical, NPCs, each of which participates in the import and export of nuclear material from within the nucleus [1–2]. Exactly how this transport occurs through the NPC is an open question, and a very important one, with profound implications for nanoscale devices for fluidic transport, genetic engineering and targeted drug delivery.
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Wang, Ying-Nai, Hirohito Yamaguchi, Longfei Huo, Yi Du, Hong-Jen Lee, Heng-Huan Lee, Hongmei Wang, Jung-Mao Hsu, and Mien-Chie Hung. "Abstract 4051: EGF receptor trafficking from the cell surface to the nucleus through the Golgi, ER, and nuclear envelope." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4051.

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Shourkaei, Seyed Mehdi Jafarnejad, Aijaz Ahmed Wani, Magdalena Martinka, and Gang Li. "Abstract 2243: Prognostic significance of nuclear Sox4 expression in cutaneous melanoma and its role in cell migration." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2243.

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Driscoll, Tristan P., Su-Jin Heo, and Robert L. Mauck. "Dynamic Tensile Loading and Altered Cell Contractility Modulate Nuclear Deformation and Cytoskeletal Connectivity." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80550.

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Effective use of progenitor cells in orthopaedic tissue engineering will require a thorough understanding of the mechanisms by which forces are transmitted and sensed, and how these change with differentiation. Nesprins are a family of structural proteins that partially localize to the nuclear envelope where they interact with both cytoskeletal and nucleoskeletal proteins [1]. At their C-terminus, nesprins interact through a KASH domain with proteins of the nuclear membrane, including SUN and Lamin A/C [1]. Multiple isoforms of the 4 nesprin genes are produced by alternative transcriptional initiation, translation and splicing. Specifically, nesprin 1 and nesprin 2 giant contain an N-terminal calponin homology domain (CH) that binds to and co-localizes with F-actin [2]. These nesprins are necessary for transmission of stress to the nucleus and are also differentially regulated with myogenesis, neurogenesis and adipogenesis [3,4]. We previously demonstrated that addition of TGF-3 induced nuclear Lamin A/C reorganization and nuclear stiffening in mesenchymal stem cells (MSCs), along with increased cell contractility and altered accumulation of smaller nesprin isoforms [5,6]. This study sought to determine the importance of contractility in transmission of force to the nucleus and the effect of dynamic loading on the expression of the giant nesprin isoforms.
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Biyik-Sit, Rumeysa, Traci Kruer, Susan M. Dougherty, James Bradley, Michael L. Merchant, John O. Trent, and Brian F. Clem. "Abstract 4933: Nuclear Pyruvate Kinase M2 (PKM2) contributes to PSAT1-mediated cell migration in EGFR-activated lung cancer cells." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-4933.

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