Toward a consensus on the mechanism of nuclear pore complex inheritance

References

• Akhtar A, Gasser SM. The nuclear envelope and transcriptional control. Nat Rev Genet 2007; 8:507 - 17; http://dx.doi.org/10.1038/nrg2122; PMID: 17549064
   PubMed Web of Science ®Google Scholar
• Köhler A, Hurt E. Gene regulation by nucleoporins and links to cancer. Mol Cell 2010; 38:6 - 15; http://dx.doi.org/10.1016/j.molcel.2010.01.040; PMID: 20385085
   PubMed Web of Science ®Google Scholar
• Fiserova J, Kiseleva E, Goldberg MW. Nuclear envelope and nuclear pore complex structure and organization in tobacco BY-2 cells. Plant J 2009; 59:243 - 55; http://dx.doi.org/10.1111/j.1365-313X.2009.03865.x; PMID: 19392704
   PubMed Web of Science ®Google Scholar
• Maeshima K, Yahata K, Sasaki Y, Nakatomi R, Tachibana T, Hashikawa T, Imamoto F, Imamoto N. Cell-cycle-dependent dynamics of nuclear pores: pore-free islands and lamins. J Cell Sci 2006; 119:4442 - 51; http://dx.doi.org/10.1242/jcs.03207; PMID: 17074834
   PubMed Web of Science ®Google Scholar
• Weiner A, Dahan-Pasternak N, Shimoni E, Shinder V, von Huth P, Elbaum M, Dzikowski R. 3D nuclear architecture reveals coupled cell cycle dynamics of chromatin and nuclear pores in the malaria parasite Plasmodium falciparum. Cell Microbiol 2011; 13:967 - 77; http://dx.doi.org/10.1111/j.1462-5822.2011.01592.x; PMID: 21501361
   PubMedGoogle Scholar
• Maul GG, Deaven LL, Freed JJ, Campbell GL, Beçak W. Investigation of the determinants of nuclear pore number. Cytogenet Cell Genet 1980; 26:175 - 90; http://dx.doi.org/10.1159/000131439; PMID: 6966999
   PubMedGoogle Scholar
• Lewin JM, Lwaleed BA, Cooper AJ, Birch BR. The direct effect of nuclear pores on nuclear chemotherapeutic concentration in multidrug resistant bladder cancer: the nuclear sparing phenomenon. J Urol 2007; 177:1526 - 30; http://dx.doi.org/10.1016/j.juro.2006.11.048; PMID: 17382772
   PubMed Web of Science ®Google Scholar
• Colombi P, Webster BM, Fröhlich F, Lusk CP. The transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1. J Cell Biol 2013; 203:215 - 32; http://dx.doi.org/10.1083/jcb.201305115; PMID: 24165936
   PubMed Web of Science ®Google Scholar
• Makio T, Lapetina DL, Wozniak RW. Inheritance of yeast nuclear pore complexes requires the Nsp1p subcomplex. J Cell Biol 2013; 203:187 - 96; http://dx.doi.org/10.1083/jcb.201304047; PMID: 24165935
   PubMed Web of Science ®Google Scholar
• Shcheprova Z, Baldi S, Frei SB, Gonnet G, Barral Y. A mechanism for asymmetric segregation of age during yeast budding. Nature 2008; 454:728 - 34; PMID: 18660802
   PubMed Web of Science ®Google Scholar
• Khmelinskii A, Keller PJ, Bartosik A, Meurer M, Barry JD, Mardin BR, Kaufmann A, Trautmann S, Wachsmuth M, Pereira G, et al. Tandem fluorescent protein timers for in vivo analysis of protein dynamics. Nat Biotechnol 2012; 30:708 - 14; http://dx.doi.org/10.1038/nbt.2281; PMID: 22729030
   PubMed Web of Science ®Google Scholar
• Khmelinskii A, Keller PJ, Lorenz H, Schiebel E, Knop M. Segregation of yeast nuclear pores. Nature 2010; 466:E1; http://dx.doi.org/10.1038/nature09255; PMID: 20651645
   PubMedGoogle Scholar
• Menendez-Benito V, van Deventer SJ, Jimenez-Garcia V, Roy-Luzarraga M, van Leeuwen F, Neefjes J. Spatiotemporal analysis of organelle and macromolecular complex inheritance. Proc Natl Acad Sci U S A 2013; 110:175 - 80; http://dx.doi.org/10.1073/pnas.1207424110; PMID: 23248297
   PubMedGoogle Scholar
• D’Angelo MA, Raices M, Panowski SH, Hetzer MW. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell 2009; 136:284 - 95; http://dx.doi.org/10.1016/j.cell.2008.11.037; PMID: 19167330
   PubMed Web of Science ®Google Scholar
• Toyama BH, Savas JN, Park SK, Harris MS, Ingolia NT, Yates JR 3rd, Hetzer MW. Identification of long-lived proteins reveals exceptional stability of essential cellular structures. Cell 2013; 154:971 - 82; http://dx.doi.org/10.1016/j.cell.2013.07.037; PMID: 23993091
   PubMed Web of Science ®Google Scholar
• Toyama BH, Hetzer MW. Protein homeostasis: live long, won’t prosper. Nat Rev Mol Cell Biol 2013; 14:55 - 61; http://dx.doi.org/10.1038/nrm3496; PMID: 23258296
   PubMed Web of Science ®Google Scholar
• Savas JN, Toyama BH, Xu T, Yates JR 3rd, Hetzer MW. Extremely long-lived nuclear pore proteins in the rat brain. Science 2012; 335:942; http://dx.doi.org/10.1126/science.1217421; PMID: 22300851
   PubMed Web of Science ®Google Scholar
• Spokoini R, Moldavski O, Nahmias Y, England JL, Schuldiner M, Kaganovich D. Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast. Cell Rep 2012; 2:738 - 47; http://dx.doi.org/10.1016/j.celrep.2012.08.024; PMID: 23022486
   PubMed Web of Science ®Google Scholar
• Bucci M, Wente SR. In vivo dynamics of nuclear pore complexes in yeast. J Cell Biol 1997; 136:1185 - 99; http://dx.doi.org/10.1083/jcb.136.6.1185; PMID: 9087436
   PubMed Web of Science ®Google Scholar
• Belgareh N, Doye V. Dynamics of nuclear pore distribution in nucleoporin mutant yeast cells. J Cell Biol 1997; 136:747 - 59; http://dx.doi.org/10.1083/jcb.136.4.747; PMID: 9049242
   PubMed Web of Science ®Google Scholar
• Daigle N, Beaudouin J, Hartnell L, Imreh G, Hallberg E, Lippincott-Schwartz J, Ellenberg J. Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells. J Cell Biol 2001; 154:71 - 84; http://dx.doi.org/10.1083/jcb.200101089; PMID: 11448991
   PubMed Web of Science ®Google Scholar
• Winey M, Yarar D, Giddings TH Jr., Mastronarde DN. Nuclear pore complex number and distribution throughout the Saccharomyces cerevisiae cell cycle by three-dimensional reconstruction from electron micrographs of nuclear envelopes. Mol Biol Cell 1997; 8:2119 - 32; http://dx.doi.org/10.1091/mbc.8.11.2119; PMID: 9362057
   PubMed Web of Science ®Google Scholar
• Niepel M, Strambio-de-Castillia C, Fasolo J, Chait BT, Rout MP. The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly. J Cell Biol 2005; 170:225 - 35; http://dx.doi.org/10.1083/jcb.200504140; PMID: 16027220
   PubMed Web of Science ®Google Scholar
• Colón-Ramos DA, Salisbury JL, Sanders MA, Shenoy SM, Singer RH, García-Blanco MA. Asymmetric distribution of nuclear pore complexes and the cytoplasmic localization of beta2-tubulin mRNA in Chlamydomonas reinhardtii. Dev Cell 2003; 4:941 - 52; http://dx.doi.org/10.1016/S1534-5807(03)00163-1; PMID: 12791277
   PubMedGoogle Scholar
• Yewdell WT, Colombi P, Makhnevych T, Lusk CP. Lumenal interactions in nuclear pore complex assembly and stability. Mol Biol Cell 2011; 22:1375 - 88; http://dx.doi.org/10.1091/mbc.E10-06-0554; PMID: 21346187
   PubMed Web of Science ®Google Scholar
• Taddei A, Gasser SM. Structure and function in the budding yeast nucleus. Genetics 2012; 192:107 - 29; http://dx.doi.org/10.1534/genetics.112.140608; PMID: 22964839
   PubMed Web of Science ®Google Scholar
• Van de Vosse DW, Wan Y, Lapetina DL, Chen W-M, Chiang J-H, Aitchison JD, Wozniak RW. A role for the nucleoporin Nup170p in chromatin structure and gene silencing. Cell 2013; 152:969 - 83; http://dx.doi.org/10.1016/j.cell.2013.01.049; PMID: 23452847
   PubMed Web of Science ®Google Scholar
• Yam C, Gu Y, Oliferenko S. Partitioning and remodeling of the Schizosaccharomyces japonicus mitotic nucleus require chromosome tethers. [Internet] Curr Biol 2013; 23:2303 - 10; http://linkinghub.elsevier.com/retrieve/pii/S0960982213012451 http://dx.doi.org/10.1016/j.cub.2013.09.057; PMID: 24184107
   PubMedGoogle Scholar
• Payne C, Rawe V, Ramalho-Santos J, Simerly C, Schatten G. Preferentially localized dynein and perinuclear dynactin associate with nuclear pore complex proteins to mediate genomic union during mammalian fertilization. [Internet] J Cell Sci 2003; 116:4727 - 38; http://jcs.biologists.org/content/116/23/4727.full http://dx.doi.org/10.1242/jcs.00784; PMID: 14600259
   PubMedGoogle Scholar
• Stelter P, Kunze R, Flemming D, Höpfner D, Diepholz M, Philippsen P, Böttcher B, Hurt E. Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex. Nat Cell Biol 2007; 9:788 - 96; http://dx.doi.org/10.1038/ncb1604; PMID: 17546040
   PubMed Web of Science ®Google Scholar
• Splinter D, Tanenbaum ME, Lindqvist A, Jaarsma D, Flotho A, Yu KL, Grigoriev I, Engelsma D, Haasdijk ED, Keijzer N, et al. Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes and regulate centrosome and nuclear positioning during mitotic entry. PLoS Biol 2010; 8:e1000350; http://dx.doi.org/10.1371/journal.pbio.1000350; PMID: 20386726
   PubMed Web of Science ®Google Scholar
• Bolhy S, Bouhlel I, Dultz E, Nayak T, Zuccolo M, Gatti X, Vallee R, Ellenberg J, Doye V. A Nup133-dependent NPC-anchored network tethers centrosomes to the nuclear envelope in prophase. J Cell Biol 2011; 192:855 - 71; http://dx.doi.org/10.1083/jcb.201007118; PMID: 21383080
   PubMed Web of Science ®Google Scholar
• Steinberg G, Schuster M, Theisen U, Kilaru S, Forge A, Martin-Urdiroz M. Motor-driven motility of fungal nuclear pores organizes chromosomes and fosters nucleocytoplasmic transport. J Cell Biol 2012; 198:343 - 55; http://dx.doi.org/10.1083/jcb.201201087; PMID: 22851316
   PubMed Web of Science ®Google Scholar
• Dilworth DJ, Suprapto A, Padovan JC, Chait BT, Wozniak RW, Rout MP, Aitchison JD. Nup2p dynamically associates with the distal regions of the yeast nuclear pore complex. J Cell Biol 2001; 153:1465 - 78; http://dx.doi.org/10.1083/jcb.153.7.1465; PMID: 11425876
   PubMed Web of Science ®Google Scholar
• Haruki H, Nishikawa J, Laemmli UK. The anchor-away technique: rapid, conditional establishment of yeast mutant phenotypes. Mol Cell 2008; 31:925 - 32; http://dx.doi.org/10.1016/j.molcel.2008.07.020; PMID: 18922474
   PubMed Web of Science ®Google Scholar
• Marguerat S, Schmidt A, Codlin S, Chen W, Aebersold R, Bähler J. Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells. Cell 2012; 151:671 - 83; http://dx.doi.org/10.1016/j.cell.2012.09.019; PMID: 23101633
   PubMed Web of Science ®Google Scholar
• Alber F, Dokudovskaya S, Veenhoff LM, Zhang W, Kipper J, Devos D, Suprapto A, Karni-Schmidt O, Williams R, Chait BT, et al. Determining the architectures of macromolecular assemblies. Nature 2007; 450:683 - 94; http://dx.doi.org/10.1038/nature06404; PMID: 18046405
   PubMed Web of Science ®Google Scholar
• Alber F, Dokudovskaya S, Veenhoff LM, Zhang W, Kipper J, Devos D, Suprapto A, Karni-Schmidt O, Williams R, Chait BT, et al. The molecular architecture of the nuclear pore complex. Nature 2007; 450:695 - 701; http://dx.doi.org/10.1038/nature06405; PMID: 18046406
   PubMed Web of Science ®Google Scholar
• Hubert T, Vandekerckhove J, Gettemans J. Exo70-mediated recruitment of nucleoporin Nup62 at the leading edge of migrating cells is required for cell migration. Traffic 2009; 10:1257 - 71; http://dx.doi.org/10.1111/j.1600-0854.2009.00940.x; PMID: 19552648
   PubMed Web of Science ®Google Scholar
• Zhou T, Li S, Zhong W, Vihervaara T, Béaslas O, Perttilä J, Luo W, Jiang Y, Lehto M, Olkkonen VM, et al. OSBP-related protein 8 (ORP8) regulates plasma and liver tissue lipid levels and interacts with the nucleoporin Nup62. PLoS One 2011; 6:e21078; http://dx.doi.org/10.1371/journal.pone.0021078; PMID: 21698267
   PubMedGoogle Scholar
• Béaslas O, Vihervaara T, Li J, Laurila P-P, Yan D, Olkkonen VM. Silencing of OSBP-related protein 8 (ORP8) modifies the macrophage transcriptome, nucleoporin p62 distribution, and migration capacity. Exp Cell Res 2012; 318:1933 - 45; http://dx.doi.org/10.1016/j.yexcr.2012.05.026; PMID: 22683860
   PubMedGoogle Scholar
• Hubert T, Van Impe K, Vandekerckhove J, Gettemans J. The actin-capping protein CapG localizes to microtubule-dependent organelles during the cell cycle. Biochem Biophys Res Commun 2009; 380:166 - 70; http://dx.doi.org/10.1016/j.bbrc.2009.01.064; PMID: 19166812
   PubMed Web of Science ®Google Scholar
• Irazoqui JE, Lew DJ. Polarity establishment in yeast. J Cell Sci 2004; 117:2169 - 71; http://dx.doi.org/10.1242/jcs.00953; PMID: 15126618
   PubMedGoogle Scholar
• Babour A, Bicknell AA, Tourtellotte J, Niwa M. A surveillance pathway monitors the fitness of the endoplasmic reticulum to control its inheritance. Cell 2010; 142:256 - 69; http://dx.doi.org/10.1016/j.cell.2010.06.006; PMID: 20619447
   PubMed Web of Science ®Google Scholar
• Patel SS, Rexach MF. Discovering novel interactions at the nuclear pore complex using bead halo: a rapid method for detecting molecular interactions of high and low affinity at equilibrium. Mol Cell Proteomics 2008; 7:121 - 31; http://dx.doi.org/10.1074/mcp.M700407-MCP200; PMID: 17897934
   PubMed Web of Science ®Google Scholar
• West M, Zurek N, Hoenger A, Voeltz GK. A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature. J Cell Biol 2011; 193:333 - 46; http://dx.doi.org/10.1083/jcb.201011039; PMID: 21502358
   PubMed Web of Science ®Google Scholar
• Kirchenbauer M, Liakopoulos D. An auxiliary, membrane-based mechanism for nuclear migration in budding yeast. Mol Biol Cell 2013; 24:1434 - 43; http://dx.doi.org/10.1091/mbc.E12-08-0602; PMID: 23447703
   PubMed Web of Science ®Google Scholar
• Prinz WA, Grzyb L, Veenhuis M, Kahana JA, Silver PA, Rapoport TA. Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae. J Cell Biol 2000; 150:461 - 74; http://dx.doi.org/10.1083/jcb.150.3.461; PMID: 10931860
   PubMed Web of Science ®Google Scholar
• Fehrenbacher KL, Davis D, Wu M, Boldogh I, Pon LA. Endoplasmic reticulum dynamics, inheritance, and cytoskeletal interactions in budding yeast. Mol Biol Cell 2002; 13:854 - 65; http://dx.doi.org/10.1091/mbc.01-04-0184; PMID: 11907267
   PubMed Web of Science ®Google Scholar