Regulation of diverse nuclear shapes: pathways working independently, together

References

• Mekhail K, Moazed D. The nuclear envelope in genome organization, expression and stability. Nat Rev Cell Biol. 2010;11(5):317–328.
   PubMed Web of Science ®Google Scholar
• Cremer T, Cremer M, Dietzel S, et al. Chromosome territories - a functional nuclear landscape. Curr Opin Cell Biol. 2006;18(3):307–316.
   PubMed Web of Science ®Google Scholar
• Méndez-lópez I, Worman HJ. Inner nuclear membrane proteins : impact on human disease. Chromosoma. 2012;121(2):153–167.
   PubMed Web of Science ®Google Scholar
• Rempel IL, Crane MM, Thaller DJ, et al. Age-dependent deterioration of nuclear pore assembly in mitotic cells decreases transport dynamics. Elife. 2019;8. DOI:https://doi.org/10.7554/eLife.48186.
   PubMed Web of Science ®Google Scholar
• Lattanzi G, Benedetti S, D’Apice MR, et al. Emerging perspectives on laminopathies. Cell Health Cytoskelet. 2016. DOI:https://doi.org/10.2147/CHC.S59507
   Google Scholar
• Alvarado-Kristensson M, Rosselló CA. The Biology of the nuclear envelope and its implications in cancer biology. Int J Mol Sci. 2019;20(10):2586.
   PubMed Web of Science ®Google Scholar
• Filesi I, Gullotta F, Lattanzi G, et al. Alterations of nuclear envelope and chromatin organization in mandibuloacral dysplasia, a rare form of laminopathy. Physiol Genomics. 2005;23(2):150–158.
   PubMed Web of Science ®Google Scholar
• Goldman RD, Shumaker DK, Erdos MR, et al. Accumulation of mutant lamin A progressive changes in nuclear architecture in Hutchinson-Gilford progeria syndrome. Proc Natl Acad Sci U S A. 2004;101(24):8963–8968.
   Web of Science ®Google Scholar
• Tolksdorf G, Stein H, Lennert K. Morphological and immunological definition of a malignant lymphoma derived from germinal-centre cells with cleaved nuclei (centrocytes). Br J Cancer. 1980;41(2):168–182.
   PubMed Web of Science ®Google Scholar
• Skinner BM, Johnson EEP. Nuclear morphologies: their diversity and functional relevance. Chromosoma. 2017;126(2):195–212.
   PubMed Web of Science ®Google Scholar
• Manley HR, Keightley MC, Lieschke GJ. The neutrophil nucleus: an important influence on neutrophil migration and function. Front Immunol. 2018;9. DOI:https://doi.org/10.3389/fimmu.2018.02867.
   Google Scholar
• Theera-Umpon N, Dhompongsa S. Morphological granulometric features of nucleus in automatic bone marrow white blood cell classification. IEEE Trans Inf Technol Biomed. 2007;11(3):353–359.
   PubMedGoogle Scholar
• Blofield BA, Short L, Samour HJ, et al. Phylogenetic and haematological implications of differences in the morphology of the heterophil nucleus in reptiles. J Zool. 1992;226(4):539–549.
   Google Scholar
• Leitch AR. Higher levels of organization in the interphase nucleus of cycling and differentiated cells. Microbiol Mol Biol Rev. 2000;64(1):138–152.
   PubMed Web of Science ®Google Scholar
• Gu N-H, Zhao W-L, Wang G-S, et al. Comparative analysis of mammalian sperm ultrastructure reveals relationships between sperm morphology, mitochondrial functions and motility. Reprod Biol Endocrinol. 2019;17(1):66.
   PubMed Web of Science ®Google Scholar
• Miller DL, Styer EL, Decker SJ, et al. Ultrastructure of the spermatozoa from three odontocetes: a killer whale (Orcinus orca), a Pacific white-sided dolphin (Lagenorhynchus obliquidens) and a beluga (Delphinapterus leucas). Anat Histol Embryol. 2002;31(3):158–168.
   PubMed Web of Science ®Google Scholar
• Santiago-Moreno J, Esteso M, Villaverde-Morcillo S, et al. Recent advances in bird sperm morphometric analysis, and its role in male gamete characterization and reproduction technologies. Asian J Androl. 2016;18(6):882–888.
   PubMed Web of Science ®Google Scholar
• Meier I, Griffis AH, Groves NR, et al. Regulation of nuclear shape and size in plants. Curr Opin Cell Biol. 2016;40:114–123.
   PubMed Web of Science ®Google Scholar
• Chytilova E, Macas J, Galbraith DW. Green fluorescent protein targeted to the nucleus, a transgenic phenotype useful for studies in plant biology. Ann Bot. 1999;83(6):645–654.
   Web of Science ®Google Scholar
• Dittmer TA, Stacey NJ, Sugimoto-Shirasu K, et al. LITTLE NUCLEI genes affecting nuclear morphology in arabidopsis thaliana. Plant Cell. 2007;19(9):2793–2803.
   PubMed Web of Science ®Google Scholar
• Collings DA, Carter CN, Rink JC, et al. Plant nuclei can contain extensive grooves and invaginations. Plant Cell. 2000. DOI:https://doi.org/10.1105/tpc.12.12.2425
   Google Scholar
• Wang R, Kamgoue A, Normand C, et al. High resolution microscopy reveals the nuclear shape of budding yeast during cell cycle and in various biological states. J Cell Sci. 2016;129(24):4480–4495.
   PubMed Web of Science ®Google Scholar
• Ketelaar T, Faivre-Moskalenko C, Esseling JJ, et al. Positioning of nuclei in arabidopsis root hairs. Plant Cell. 2002;14(11):2941–2955.
   PubMed Web of Science ®Google Scholar
• Brandt A, Papagiannouli F, Wagner N, et al. Developmental control of nuclear size and shape by kugelkern and kurzkern. Curr Biol. 2006;16(6):543–552.
   PubMed Web of Science ®Google Scholar
• Webster M, Wikin KL, Cohen-Fix O. Sizing up the nucleus: nuclear shape, size and nuclear-envelope assembly. J Cell Sci. 2009;122(10):1477–1486.
   PubMed Web of Science ®Google Scholar
• Schreiner SM, Koo PK, Zhao Y, et al. The tethering of chromatin to the nuclear envelope supports nuclear mechanics. Nat Commun. 2015;6(1):7159.
   PubMedGoogle Scholar
• Stephens AD, Banigan EJ, Marko JF. Chromatin’s physical properties shape the nucleus and its functions. Curr Opin Cell Biol. 2019;58:76–84.
   PubMed Web of Science ®Google Scholar
• Titus LC, Dawson TR, Rexer DJ, et al. Members of the RSC chromatin-remodeling complex are required for maintaining proper nuclear envelope structure and pore complex localization. Mol Biol Cell. 2010;21(6):1072–1087.
   PubMed Web of Science ®Google Scholar
• Jin QW, Fuchs J, Loidl J. Centromere clustering is a major determinant of yeast interphase nuclear organization. J Cell Sci. 2000;113(11):1903–1912.
   PubMed Web of Science ®Google Scholar
• Wang R, Mozziconacci J, Bancaud A, et al. Principles of chromatin organization in yeast: relevance of polymer models to describe nuclear organization and dynamics. Curr Opin Cell Biol. 2015;34:54–60.
   PubMed Web of Science ®Google Scholar
• Sáez-Vásquez J, Gadal O. Genome organization and function: a view from yeast and arabidopsis. Mol Plant. 2010;3(4):678–690.
   PubMed Web of Science ®Google Scholar
• Mekhail K, Seebacher J, Gygi SP, et al. Role for perinuclear chromosome tethering in maintenance of genome stability. Nature. 2008;456(7222):667–670.
   PubMed Web of Science ®Google Scholar
• Tiang CL, He Y, Pawlowski WP. Chromosome organization and dynamics during interphase, mitosis, and meiosis in plants. Plant Physiol. 2012;158(1):26–34.
   PubMed Web of Science ®Google Scholar
• Poulet A, Duc C, Voisin M, et al. The LINC complex contributes to heterochromatin organisation and transcriptional gene silencing in plants. J Cell Sci. 2017. doi:https://doi.org/10.1242/jcs.194712
   Google Scholar
• Cr C, Br C. The biology of chromatin remodeling complexes. Annu Rev Biochem. 2009;78:273–304
   PubMed Web of Science ®Google Scholar
• Imbalzano KM, Cohet N, Wu Q, et al. Nuclear shape changes are induced by knockdown of the SWI/SNF ATPase BRG1 and are independent of cytoskeletal connections. PLoS One. 2013;8(2):e55628.
   PubMed Web of Science ®Google Scholar
• Shang E, Nickerson HD, Wen D, et al. The first bromodomain of Brdt, a testis-specific member of the BET sub-family of double-bromodomain-containing proteins, is essential for male germ cell differentiation. Development. 2007;134(19):3507–3515.
   PubMed Web of Science ®Google Scholar
• Pinheiro I, Margueron R, Shukeir N, et al. Prdm3 and Prdm16 are H3K9me1 methyltransferases required for mammalian heterochromatin integrity. Cell. 2012;150(5):948–960.
   PubMed Web of Science ®Google Scholar
• Pawar V, Poulet A, Détourné G, et al. A novel family of plant nuclear envelope-associated proteins. J Exp Bot. 2016;67:5699–5710.
   PubMed Web of Science ®Google Scholar
• Laporte D, Courtout F, Tollis S, et al. Quiescent Saccharomyces cerevisiae forms telomere hyperclusters at the nuclear membrane vicinity through a multifaceted mechanism involving Esc1, the Sir complex, and chromatin condensation. Mol Biol Cell. 2016;27(12):1875–1884.
   PubMed Web of Science ®Google Scholar
• Male G, Deolal P, Manda NK, et al. Nucleolar size regulates nuclear envelope shape in Saccharomyces cerevisiae. J Cell Sci. 2020. DOI:https://doi.org/10.1242/jcs.242172
   PubMed Web of Science ®Google Scholar
• Taddei A, Gasser SM. Structure and function in the budding yeast nucleus. Genetics. 2012;192(1):107–129.
   PubMed Web of Science ®Google Scholar
• Dechat T, Adam SA, Taimen P, et al. Nuclear lamins. Cold Spring Harb Perspect Biol. 2010;2(11):a000547.
   PubMed Web of Science ®Google Scholar
• Dittmer T, Misteli T. The lamin protein family. Genome Biol. 2011;12(5):222.
   PubMed Web of Science ®Google Scholar
• Taimen P, Pfleghaar K, Shimi T, et al. A progeria mutation reveals functions for lamin A in nuclear assembly, architecture, and chromosome organization. Proc Natl Acad Sci. 2009;106(49):20788–20793.
   PubMed Web of Science ®Google Scholar
• Scaffidi P, Misteli T. Lamin A-dependent nuclear defects in human aging. Science. 2006;312(5776):1059–1063.
   PubMed Web of Science ®Google Scholar
• Pathak RU, Soujanya M, Mishra RK. Deterioration of nuclear morphology and architecture: a hallmark of senescence and aging. Ageing Res Rev. 2021;67:101264.
   PubMed Web of Science ®Google Scholar
• Lenz-Böhme B, Wismar J, Fuchs S, et al. Insertional mutation of the drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae. J Cell Biol. 1997;137(5):1001–1016.
   PubMed Web of Science ®Google Scholar
• Liu J, Ben-Shahar TR, Riemer D, et al. Essential roles for caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes. Mol Biol Cell. 2000;11(11):3937–3947.
   PubMed Web of Science ®Google Scholar
• Masuda K, Takahashi S, Nomura K, et al. Residual structure and constituent proteins of the peripheral framework of the cell nucleus in somatic embryos from Daucus carota L. Planta. 1993;191(4). DOI:https://doi.org/10.1007/BF00195755
   Google Scholar
• Masuda K, Xu ZJ, Takahashi S, et al. Peripheral framework of carrot cell nucleus contains a novel protein predicted to exhibit a long α-helical domain. Exp Cell Res. 1997;232(1):173–181.
   PubMed Web of Science ®Google Scholar
• Sakamoto Y, Takagi S. LITTLE NUCLEI 1 and 4 regulate nuclear morphology in arabidopsis thaliana. Plant Cell Physiol. 2013;54(4):622–633.
   Web of Science ®Google Scholar
• Hu B, Wang N, Bi X, et al. Plant lamin-like proteins mediate chromatin tethering at the nuclear periphery. Genome Biol. 2019a;20(1):87.
   PubMed Web of Science ®Google Scholar
• Ciska M, Masuda K, Moreno Díaz de la Espina S. Characterization of the lamin analogue NMCP2 in the monocot Allium cepa. Chromosoma. 2018;127(1):103–113.
   PubMed Web of Science ®Google Scholar
• Ciska M, Masuda K, Moreno Díaz De La Espina S. Lamin-like analogues in plants: the characterization of NMCP1 in Allium cepa. J Exp Bot. 2013;64(6):1553–1564.
   PubMed Web of Science ®Google Scholar
• Blunt EL, Shandler JA, Hughes EJ, et al. Coordination of NMCP1- and NMCP2-class proteins within the plant nucleoskeleton. Mol Biol Cell. 2020;mbc.E19-08-0464. DOI:https://doi.org/10.1091/mbc.e19-08-0464
   Google Scholar
• Melcer S, Gruenbaum Y, Krohne G. Invertebrate lamins. Exp Cell Res. 2007;313(10):2157–2166.
   PubMed Web of Science ®Google Scholar
• Riemer D, Wang J, Zimek A, et al. Tunicates have unusual nuclear lamins with a large deletion in the carboxyterminal tail domain. Gene. 2000;255(2):317–325.
   PubMed Web of Science ®Google Scholar
• Andrulis ED, Zappulla DC, Ansari A, et al. Esc1, a nuclear periphery protein required for Sir4-based plasmid anchoring and partitioning. Mol Cell Biol. 2002;22(23):8292–8301.
   PubMed Web of Science ®Google Scholar
• Hattier T, Andrulis ED, Tartakoff AM. Immobility, inheritance and plasticity of shape of the yeast nucleus. BMC Cell Biol. 2007;8(1):47.
   PubMedGoogle Scholar
• Garapati HS, Mishra K. Comparative genomics of nuclear envelope proteins. BMC Genomics. 2018;19(1):823.
   PubMedGoogle Scholar
• Horigome C, Mizuta K. Ribosome biogenesis factors working with a nuclear envelope SUN domain protein. Nucleus. 2012;3(1):22–28.
   PubMed Web of Science ®Google Scholar
• DuBois KN, Alsford S, Holden JM, et al. NUP-1 is a large coiled-coil nucleoskeletal protein in trypanosomes with lamin-like functions. PLoS Biol. 2012;10(3):e1001287.
   PubMed Web of Science ®Google Scholar
• Galy V, Askjaer P, Franz C, et al. MEL-28, a novel nuclear-envelope and kinetochore protein essential for zygotic nuclear-envelope assembly in C. elegans. Curr Biol. 2006;16(17):1748–1756.
   PubMed Web of Science ®Google Scholar
• Mínguez A, Franca S, Moreno Díaz De La Espina S. Dinoflagellates have a eukaryotic nuclear matrix with lamin-like proteins and topoisomerase II. J Cell Sci. 1994;107(10):2861–2873.
   PubMedGoogle Scholar
• Krüger A, Batsios P, Baumann O, et al. Characterization of NE81, the first lamin-like nucleoskeleton protein in a unicellular organism. Mol Biol Cell. 2012;23(2):360–370.
   PubMed Web of Science ®Google Scholar
• Iwamoto M, Hiraoka Y, Haraguchi T. Uniquely designed nuclear structures of lower eukaryotes. Curr Opin Cell Biol. 2016;40:66–73.
   PubMed Web of Science ®Google Scholar
• Suga H, Chen Z, De Mendoza A, et al. The Capsaspora genome reveals a complex unicellular prehistory of animals. Nat Commun. 2013;4(1):2325.
   PubMedGoogle Scholar
• Banday S, Farooq Z, Rashid R, et al. Role of inner nuclear membrane protein complex Lem2-Nur1 in heterochromatic gene silencing. J Biol Chem. 2016;291(38):20021–20029.
   PubMed Web of Science ®Google Scholar
• Cai M, Huang Y, Ghirlando R, et al. Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA. EMBO J. 2001;20(16):4399–4407.
   Web of Science ®Google Scholar
• Laguri C, Gilquin B, Wolff N, et al. Structural characterization of the LEM motif common to three human inner nuclear membrane proteins. Structure. 2001;9(6):503–511.
   PubMed Web of Science ®Google Scholar
• Lin F, Blake DL, Callebaut I, et al. MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin. J Biol Chem. 2000. DOI:https://doi.org/10.1074/jbc.275.7.4840
   Google Scholar
• Mans BJ, Anantharaman V, Aravind L, et al. Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex. Cell Cycle. 2004. DOI:https://doi.org/10.4161/cc.3.12.1316
   Google Scholar
• Webster BM, Colombi P, Jäger J, et al. Surveillance of nuclear pore complex assembly by ESCRT-III/Vps4. Cell. 2014;159(2):388–401.
   PubMed Web of Science ®Google Scholar
• Webster BM, Thaller DJ, Jäger J, et al. Chm7 and Heh1 collaborate to link nuclear pore complex quality control with nuclear envelope sealing. EMBO J. 2016;35(22):2447–2467.
   PubMed Web of Science ®Google Scholar
• Yewdell WT, Colombi P, Makhnevych T, et al. Lumenal interactions in nuclear pore complex assembly and stability. Mol Biol Cell. 2011;22(8):1375–1388.
   PubMed Web of Science ®Google Scholar
• King MC, Drivas TG, Blobel G. A network of nuclear envelope membrane proteins linking centromeres to microtubules. Cell. 2008;134(3):427–438.
   PubMed Web of Science ®Google Scholar
• Gonzalez Y, Saito A, Sazer S. Fission yeast Lem2 and Man1 perform fundamental functions of the animal cell nuclear lamina. Nucleus. 2012;3(1):60–76.
   PubMed Web of Science ®Google Scholar
• Hu C, Inoue H, Sun W, et al. The inner nuclear membrane protein Bqt4 in fission yeast contains a DNA-binding domain essential for telomere association with the nuclear envelope. Structure. 2019b;27(2):335–343.e3.
   Web of Science ®Google Scholar
• Kinugasa Y, Hirano Y, Sawai M, et al. The very-long-chain fatty acid elongase Elo2 rescues lethal defects associated with loss of the nuclear barrier function in fission yeast cells. J Cell Sci. 2019;132(10). DOI:https://doi.org/10.1242/jcs.229021
   Google Scholar
• Morales-Martínez A, Dobrzynska A, Askjaer P. Inner nuclear membrane protein LEM-2 is required for correct nuclear separation and morphology in C. elegans. J Cell Sci. 2015. DOI:https://doi.org/10.1242/jcs.164202
   Google Scholar
• Kim DI, Kc B, Roux KJ. Making the LINC: SUN and KASH protein interactions. Biol Chem. 2015. DOI:https://doi.org/10.1515/hsz-2014-0267
   Google Scholar
• Rothballer A, Kutay U. The diverse functional LINCs of the nuclear envelope to the cytoskeleton and chromatin. Chromosoma. 2013;122(5):415–429.
   PubMed Web of Science ®Google Scholar
• Tatout C, Evans DE, Vanrobays E, et al. The plant LINC complex at the nuclear envelope. Chromosom Res. 2014;22(2):241–252.
   PubMed Web of Science ®Google Scholar
• Liu Q, Pante N, Misteli T, et al. Functional association of Sun1 with nuclear pore complexes. J Cell Biol. 2007;178(5):785–798.
   PubMed Web of Science ®Google Scholar
• Lombardi ML, Jaalouk DE, Shanahan CM, et al. The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton. J Biol Chem. 2011;286(30):26743–26753.
   PubMed Web of Science ®Google Scholar
• Xiong H, Rivero F, Euteneuer U, et al. Dictyostelium Sun-1 connects the centrosome to chromatin and ensures genome stability. Traffic. 2008;9(5):708–724.
   PubMed Web of Science ®Google Scholar
• Friederichs JM, Ghosh S, Smoyer CJ, et al. The SUN protein Mps3 is required for spindle pole body insertion into the nuclear membrane and nuclear envelope homeostasis. PLoS Genet. 2011;7(11):e1002365.
   PubMed Web of Science ®Google Scholar
• Lüke Y, Zaim H, Karakesisoglou I, et al. Nesprin-2 giant (NUANCE) maintains nuclear envelope architecture and composition in skin. J Cell Sci. 2008;121(11):1887–1898.
   Web of Science ®Google Scholar
• Oda Y, Fukuda H. Dynamics of Arabidopsis SUN proteins during mitosis and their involvement in nuclear shaping. Plant J. 2011;66(4):629–641.
   PubMed Web of Science ®Google Scholar
• Zhou X, Graumann K, Evans DE, et al. Novel plant SUN–KASH bridges are involved in RanGAP anchoring and nuclear shape determination. J Cell Biol. 2012;196(2):203–211.
   PubMed Web of Science ®Google Scholar
• Zhou X, Graumann K, Wirthmueller L, et al. Identification of unique SUN-interacting nuclear envelope proteins with diverse functions in plants. J Cell Biol. 2014;205:677–692.
   PubMed Web of Science ®Google Scholar
• Graumann K, Vanrobays E, Tutois S, et al. Characterization of two distinct subfamilies of SUN-domain proteins in arabidopsis and their interactions with the novel KASH-domain protein AtTIK. J Exp Bot. 2014;65(22):6499–6512.
   PubMed Web of Science ®Google Scholar
• Bahmanyar S, Schlieker C. 2020. Lipid and protein dynamics that shape nuclear envelope identity. 31. American Society for Cell Biology
   Google Scholar
• Yang HJ, Iwamoto M, Hiraoka Y, et al. Function of nuclear membrane proteins in shaping the nuclear envelope integrity during closed mitosis. J Biochem. 2017;161(6):471–477.
   Web of Science ®Google Scholar
• Jaspersen SL, Winey M. The budding yeast spindle pole body: structure, duplication, and function. Annu Rev Cell Dev Biol. 2004;20(1):1–28.
   PubMedGoogle Scholar
• Byers B, Goetsch L. Duplication of spindle plaques and integration of the yeast cell cycle. Cold Spring Harb Symp Quant Biol. 1974;38:123–131.
   PubMedGoogle Scholar
• Gonzalez Y, Meerbrey K, Chong J, et al. Nuclear shape, growth and integrity in the closed mitosis of fission yeast depend on the Ran-GTPase system, the spindle pole body and the endoplasmic reticulum. J Cell Sci. 2009;122(14):2464–2472.
   Web of Science ®Google Scholar
• Zheng L, Schwartz C, Magidson V, et al. The spindle pole bodies facilitate nuclear envelope division during closed mitosis in fission yeast. PLoS Biol. 2007;5(7):e170.
   PubMed Web of Science ®Google Scholar
• Cantwell H, Nurse P, Skotheim JM. A systematic genetic screen identifies essential factors involved in nuclear size control. PLOS Genet. 2019;15(2):e1007929.
   PubMed Web of Science ®Google Scholar
• Fernandez-Martinez J, Rout MP. Nuclear pore complex biogenesis. Curr Opin Cell Biol. 2009;21(4):603–612.
   PubMed Web of Science ®Google Scholar
• Maeshima K, Yahata K, Sasaki Y, et al. Cell-cycle-dependent dynamics of nuclear pores: pore-free islands and lamins. J Cell Sci. 2006;119(21):4442–4451.
   PubMed Web of Science ®Google Scholar
• De Magistris P, Antonin W. The dynamic nature of the nuclear envelope. Curr Biol. 2018;28(8):R487–R497.
   PubMed Web of Science ®Google Scholar
• Mészáros N, Cibulka J, Mendiburo MJ, et al. Nuclear pore basket proteins are tethered to the nuclear envelope and can regulate membrane curvature. Dev Cell. 2015;33(3):285–298.
   PubMed Web of Science ®Google Scholar
• Kim SJ, Fernandez-Martinez J, Sampathkumar P, et al. Integrative structure-function mapping of the nucleoporin Nup133 suggests a conserved mechanism for membrane anchoring of the nuclear pore complex. Mol Cell Proteomics. 2014;13(11):2911–2926.
   PubMed Web of Science ®Google Scholar
• Cohen M, Feinstein N, Wilson KL, et al. Nuclear pore protein gp210 is essential for viability in HeLa cells and caenorhabditis elegans. Mol Biol Cell. 2003;14(10):4230–4237.
   PubMed Web of Science ®Google Scholar
• Antonin W, Franz C, Haselmann U, et al. The integral membrane nucleoporin pom121 functionally links nuclear pore complex assembly and nuclear envelope formation. Mol Cell. 2005;17(1):83–92.
   PubMed Web of Science ®Google Scholar
• Yavuz S, Santarella-Mellwig R, Koch B, et al. NLS-mediated NPC functions of the nucleoporin Pom121. FEBS Lett. 2010;584(15):3292–3298.
   PubMed Web of Science ®Google Scholar
• Clever M, Funakoshi T, Mimura Y, et al. The nucleoporin ELYS/Mel28 regulates nuclear envelope subdomain formation in HeLa cells. Nucleus. 2012;3(2):187–199.
   PubMed Web of Science ®Google Scholar
• Zhou L, Panté N. The nucleoporin Nup153 maintains nuclear envelope architecture and is required for cell migration in tumor cells. FEBS Lett. 2010;584(14):3013–3020.
   PubMed Web of Science ®Google Scholar
• Hawryluk-Gara LA, Shibuya EK, Wozniak RW. Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex. Mol Biol Cell. 2005;16(5):2382–2394.
   PubMed Web of Science ®Google Scholar
• Wente SR, Blobel G. 1990. A temperature-sensitive NUPll6 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic.
   Google Scholar
• Marelli M, Lusk CP, Chan H, et al. A link between the synthesis of nucleoporins and the biogenesis of the nuclear envelope. J Cell Biol. 2001;153(4):709–724.
   PubMed Web of Science ®Google Scholar
• Tamura K, Fukao Y, Iwamoto M, et al. Identification and characterization of nuclear pore complex components in Arabidopsis thaliana. Plant Cell. 2010;22(12):4084–4097.
   PubMed Web of Science ®Google Scholar
• Tamura K, Hara-Nishimura I. Involvement of the nuclear pore complex in morphology of the plant nucleus. Nucleus. 2011;2(3):168–172.
   PubMed Web of Science ®Google Scholar
• Dawson TR, Lazarus MD, Hetzer MW, et al. ER membrane-bending proteins are necessary for de novo nuclear pore formation. J Cell Biol. 2009;184(5):659–675.
   PubMed Web of Science ®Google Scholar
• Anderson DJ, Hetzer MW. Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation. J Cell Biol. 2008;182(5):911–924.
   PubMed Web of Science ®Google Scholar
• Goodchild RE, Kim CE, Dauer WT. Loss of the dystonia-associated protein torsinA selectively disrupts the neuronal nuclear envelope. Neuron. 2005;48(6):923–932.
   PubMed Web of Science ®Google Scholar
• Laudermilch E, Tsai PL, Graham M, et al. Dissecting Torsin/cofactor function at the nuclear envelope: a genetic study. Mol Biol Cell. 2016;27(25):3964–3971.
   PubMed Web of Science ®Google Scholar
• Rampello AJ, Laudermilch E, Vishnoi N, et al. Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of MLF2. J Cell Biol. 2020;219(6). DOI:https://doi.org/10.1083/JCB.201910185
   Google Scholar
• VanGompel MJW, Nguyen KCQ, Hall DH, et al. A novel function for the Caenorhabditis elegans torsin OOC-5 in nucleoporin localization and nuclear import. Mol Biol Cell. 2015;26(9):1752–1763.
   PubMed Web of Science ®Google Scholar
• Gu M, LaJoie D, Chen OS, et al. LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission yeast and human cells. Proc Natl Acad Sci. 2017;114(11):E2166–E2175.
   PubMed Web of Science ®Google Scholar
• Wente SR, Blobel G. A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic. J Cell Biol. 1993;123(2):275–284.
   PubMed Web of Science ®Google Scholar
• Lussi YC, Hügi I, Laurell E, et al. The nucleoporin Nup88 is interacting with nuclear lamin A. Mol Biol Cell. 2011;22(7):1080–1090.
   PubMed Web of Science ®Google Scholar
• Dazzoni R, Grélard A, Morvan E, et al. The unprecedented membrane deformation of the human nuclear envelope, in a magnetic field, indicates formation of nuclear membrane invaginations. Sci Rep. 2020;10(1). DOI:https://doi.org/10.1038/s41598-020-61746-0
   Google Scholar
• Merta H, Bahmanyar S. The inner nuclear membrane takes on lipid metabolism. Dev Cell. 2018;47(4):397–399.
   PubMed Web of Science ®Google Scholar
• Ungricht R, Kutay U. Mechanisms and functions of nuclear envelope remodelling. Nat Rev Mol Cell Biol. 2017;18(4):229–245.
   PubMed Web of Science ®Google Scholar
• Makarova M, Gu Y, Chen JS, et al. Temporal regulation of lipin activity diverged to account for differences in mitotic programs. Curr Biol. 2016;26(2):237–243.
   PubMed Web of Science ®Google Scholar
• Barbosa AD, Lim K, Mari M, et al. Compartmentalized synthesis of triacylglycerol at the inner nuclear membrane regulates nuclear organization. Dev Cell. 2019;50(6):755–766.e6.
   PubMed Web of Science ®Google Scholar
• Romanauska A, Köhler A. The inner nuclear membrane is a metabolically active territory that generates nuclear lipid droplets. Cell. 2018;174(3):700–715.e18.
   PubMed Web of Science ®Google Scholar
• Uzbekov R, Roingeard P. Nuclear lipid droplets identified by electron microscopy of serial sections. BMC Res Notes. 2013. DOI:https://doi.org/10.1186/1756-0500-6-386
   Google Scholar
• Santos-Rosa H, Leung J, Grimsey N, et al. The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth. EMBO J. 2005;24:1931–1941.
   PubMed Web of Science ®Google Scholar
• Siniossoglou S, Santos‐Rosa H, Rappsilber J, et al. A novel complex of membrane proteins required for formation of a spherical nucleus. 1998;17::6449–6464.
   Google Scholar
• Lone MA, Atkinson AE, Hodge CA, et al. Yeast integral membrane proteins Apq12, Brl1, and Brr6 form a complex important for regulation of membrane homeostasis and nuclear pore complex biogenesis. Eukaryot Cell. 2015;14(12):1217–1227.
   PubMedGoogle Scholar
• Scarcelli JJ, Hodge CA, Cole CN. The yeast integral membrane protein Apq12 potentially links membrane dynamics to assembly of nuclear pore complexes. J Cell Biol. 2007;178(5):799–812.
   PubMed Web of Science ®Google Scholar
• Han G-S-S, O’Hara L, Carman GM, et al. An unconventional diacylglycerol kinase that regulates phospholipid synthesis and nuclear membrane growth. J Biol Chem. 2008;283(29):20433–20442.
   PubMed Web of Science ®Google Scholar
• Campbell JL, Lorenz A, Witkin KL, et al. Yeast nuclear envelope subdomains with distinct abilities to resist membrane expansion. Mol Biol Cell. 2006;17(4):1768–1778.
   PubMed Web of Science ®Google Scholar
• Witkin KL, Chong Y, Shao S, et al. The budding yeast nuclear envelope adjacent to the nucleolus serves as a membrane sink during mitotic delay. Curr Biol. 2012;22(12):1128–1133.
   PubMed Web of Science ®Google Scholar
• Deolal P, Male G, Mishra K. The challenge of staying in shape: nuclear size matters. Curr Genet. 2021;67(1):1–8.
   PubMedGoogle Scholar
• Walters AD, Bommakanti A, Cohen-Fix O. Shaping the nucleus: factors and forces. J Cell Biochem. 2012;113(9):2813–2821.
   PubMed Web of Science ®Google Scholar
• Walters AD, Amoateng K, Wang R, et al. Nuclear envelope expansion in budding yeast is independent of cell growth and does not determine nuclear volume. Mol Biol Cell. 2019;30(1):131–145.
   PubMed Web of Science ®Google Scholar
• Levy DL, Heald R. Nuclear size is regulated by importin α and Ntf2 in Xenopus. Cell. 2010;143(2):288–298.
   PubMed Web of Science ®Google Scholar
• Kume K, Cantwell H, Neumann FR, et al. A systematic genomic screen implicates nucleocytoplasmic transport and membrane growth in nuclear size control. PLOS Genet. 2017;13(5):e1006767.
   PubMed Web of Science ®Google Scholar
• Chen B, Co C, Ho -C-C. Cell shape dependent regulation of nuclear morphology. Biomaterials. 2015;67:129–136.
   PubMed Web of Science ®Google Scholar
• Hobson CM, Kern M, O’Brien ET, et al. Correlating nuclear morphology and external force with combined atomic force microscopy and light sheet imaging separates roles of chromatin and lamin A/C in nuclear mechanics. Mol Biol Cell. 2020;31(16):1788–1801.
   PubMed Web of Science ®Google Scholar
• Makhija E, Jokhun DS, Shivashankar GV. Nuclear deformability and telomere dynamics are regulated by cell geometric constraints. Proc Natl Acad Sci U S A. 2016;113(1):E32–E40.
   PubMed Web of Science ®Google Scholar
• Chytilova E, Macas J, Sliwinska E, et al. Nuclear dynamics in arabidopsis thaliana. Mol Biol Cell. 2000;11(8):2733–2741.
   PubMed Web of Science ®Google Scholar
• Katsuta J, Shibaoka H. The roles of the cytoskeleton and the cell wall in nuclear positioning in tobacco BY-2 cells. Plant Cell Physiol. 1988. DOI:https://doi.org/10.1093/oxfordjournals.pcp.a077508
   Google Scholar
• Alcorta-Sevillano N, Macías I, Rodríguez CI, et al. Crucial role of Lamin A/C in the migration and differentiation of MSCs in bone. Cells. 2020;9(6):1330.
   Web of Science ®Google Scholar
• Barzilai S, Yadav SK, Morrell S, et al. Leukocytes breach endothelial barriers by insertion of nuclear lobes and disassembly of endothelial actin filaments. Cell Rep. 2017;18(3):685–699.
   PubMed Web of Science ®Google Scholar
• Lahoz-Beneytez J, Elemans M, Zhang Y, et al. Human neutrophil kinetics: modeling of stable isotope labeling data supports short blood neutrophil half-lives. Blood. 2016;127(26):3431–3438.
   PubMed Web of Science ®Google Scholar
• Rowat AC, Jaalouk DE, Zwerger M, et al. Nuclear envelope composition determines the ability of neutrophil-type cells to passage through micron-scale constrictions*. J Biol Chem. 2013;288(12):8610–8618.
   PubMed Web of Science ®Google Scholar
• Tran JR, Zheng X, Zheng Y. Lamin-B1 contributes to the proper timing of epicardial cell migration and function during embryonic heart development. Mol Biol Cell. 2016;27(25):3956–3963.
   Web of Science ®Google Scholar
• Coffinier C, Fong LG, Young SG. LINCing lamin B2 to neuronal migration, growing evidence for cell-specific roles of B-types lamins. Nucleus. 2010;1(5):407–411.
   PubMed Web of Science ®Google Scholar
• Coffinier C, Jung HJ, Nobumori C, et al. Deficiencies in lamin B1 and lamin B2 cause neurodevelopmental defects and distinct nuclear shape abnormalities in neurons. Mol Biol Cell. 2011;22(23):4683–4693.
   PubMed Web of Science ®Google Scholar
• Ji JY, Lee RT, Vergnes L, et al. Cell nuclei spin in the absence of lamin B1. J Biol Chem. 2007;282(27):20015–20026.
   Web of Science ®Google Scholar
• Fracchia A, Asraf T, Salmon-Divon M, et al. Increased Lamin B1 levels promote cell migration by altering perinuclear actin organization. Cells. 2020;9(10):2161.
   PubMed Web of Science ®Google Scholar
• Guerreiro I, Kind J. Spatial chromatin organization and gene regulation at the nuclear lamina. Curr Opin Genet Dev. 2019;55:19–25.
   PubMed Web of Science ®Google Scholar
• Zink D, Fischer AH, Nickerson JA. Nuclear structure in cancer cells. Nat Rev Cancer. 2004;4(9):677–687.
   PubMed Web of Science ®Google Scholar
• Janin A, Bauer D, Ratti F, et al. Nuclear envelopathies: a complex LINC between nuclear envelope and pathology. Orphanet J Rare Dis. 2017;12(1):147.
   PubMed Web of Science ®Google Scholar
• Worman HJ, Ostlund C, Wang Y. Diseases of the nuclear envelope. Cold Spring Harb Perspect Biol. 2010;2(2):a000760.
   PubMed Web of Science ®Google Scholar
• Matsuoka M. Human T-cell leukemia virus type I (HTLV-I) infection and the onset of adult T-cell leukemia (ATL). Retrovirology. 2005;2(1):27.
   Google Scholar
• De Noronha CMC, Sherman MP, Lin HW, et al. Dynamic disruptions in nuclear envelope architecture and integrity induced by HIV-1 Vpr. Science. 2001;294(5544):1105–1108.
   PubMed Web of Science ®Google Scholar
• Donahue DA, Amraoui S, di Nunzio F, et al. SUN2 overexpression deforms nuclear shape and inhibits HIV. J Virol. 2016;90(8):4199–4214.
   Web of Science ®Google Scholar
• Castro-Garza J, Luévano-Martínez ML, Villarreal-Treviño L, et al. Mycobacterium tuberculosis promotes genomic instability in macrophages. Mem Inst Oswaldo Cruz. 2018;113(3):161–166.
   PubMed Web of Science ®Google Scholar
• Dundr M, Misteli T. Biogenesis of nuclear bodies. Cold Spring Harb Perspect Biol. 2010;2(12):a000711–a000711.
   PubMed Web of Science ®Google Scholar
• Hariri H, Rogers S, Ugrankar R, et al. Lipid droplet biogenesis is spatially coordinated at ER–vacuole contacts under nutritional stress. EMBO Rep. 2018;19(1):57–72.
   PubMed Web of Science ®Google Scholar
• Schneiter R, Hitomi M, Ivessa AS, et al. A yeast acetyl coenzyme a carboxylase mutant links very-long-chain fatty acid synthesis to the structure and function of the nuclear membrane-pore complex. Mol Cell Biol. 1996;16(12):7161–7172.
   PubMed Web of Science ®Google Scholar
• Wright R, Basson M, D’Ari L, et al. Increased amounts of HMG-CoA reductase induce "karmellae": a proliferation of stacked membrane pairs surrounding the yeast nucleus. J Cell Biol. 1988;107(1):101–114.
   PubMed Web of Science ®Google Scholar
• Wang H, Dittmer TA, Richards EJ. Arabidopsis CROWDED NUCLEI (CRWN) proteins are required for nuclear size control and heterochromatin organization. BMC Plant Biol. 2013;13(1):200.
   Google Scholar
• Goto C, Tamura K, Fukao Y, et al. The novel nuclear envelope protein KAKU4 modulates nuclear morphology in arabidopsis. Plant Cell. 2014;26(5):2143–2155.
   PubMed Web of Science ®Google Scholar
• Polychronidou M, Grobhans J. Determining nuclear shape: the role of farnesylated nuclear membrane proteins. Nucleus. 2011;2(1):17–23.
   PubMed Web of Science ®Google Scholar
• Sullivan T, Escalante-Alcalde D, Bhatt H, et al. Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. J Cell Biol. 1999;147(5):913–920.
   PubMed Web of Science ®Google Scholar
• Zhou C, Li C, Zhou B, et al. Novel nesprin-1 mutations associated with dilated cardiomyopathy cause nuclear envelope disruption and defects in myogenesis. Hum Mol Genet. 2017;26(12):2258–2276.
   Web of Science ®Google Scholar