Abstract
Nuclear pore complexes (NPCs) are large protein complex assemblies by about 30 different proteins, called nucleoporins (Nups), embedded in the nuclear envelope. Most of transport of molecules between cytoplasm and nucleus occurs through the NPCs. The research of yeast and vertebrate NPC structure made big progress in the past decades. This chapter first reviews recent advances of NPC structure and architecture by electron microscopy and super-resolution and then further overviews the progress of NPC structure and dynamic in living yeast cells by a single molecular detection approach called single-point edge-excitation sub-diffraction (SPEED) microscopy. In the last section, we will discuss the perspective about the structure of yeast NPCs.
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References
Aitchison JD, Rout MP (2012) The yeast nuclear pore complex and transport through it. Genetics 190:855–883
Aitchison JD, Rout MP, Marelli M, Blobel G, Wozniak RW (1995) 2 novel related yeast nucleoporins Nup170P and Nup157P – complementation with the vertebrate homolog Nup155P and functional interactions with the yeast nuclear pore-membrane protein POM152P. J Cell Biol 131:1133–1148
Alber F, Dokudovskaya S, Veenhoff LM, Zhang W, Kipper J, Devos D, Suprapto A, Karni-Schmidt O, Williams R, Chait BT et al (2007) Determining the architectures of macromolecular assemblies. Nature 450:683–694
Anderson TM, Clay MC, Cioffi AG, Diaz KA, Hisao GS, Tuttle MD, Nieuwkoop AJ, Comellas G, Maryum N, Wang S et al (2014) Amphotericin forms an extramembranous and fungicidal sterol sponge. Nat Chem Biol 10:400–406
Brohawn SG, Partridge JR, Whittle JRR, Schwartz TU (2009) The nuclear pore complex has entered the atomic age. Structure 17:1156–1168
Bui KH, von Appen A, DiGuilio AL, Ori A, Sparks L, Mackmull MT, Bock T, Hagen W, Andres-Pons A, Glavy JS et al (2013) Integrated structural analysis of the human nuclear pore complex scaffold. Cell 155:1233–1243
Chang HC, Kaiser CM, Hartl FU, Barral JM (2005) De novo folding of GFP fusion proteins: high efficiency in eukaryotes but not in bacteria. J Mol Biol 353:397–409
Cronshaw JA, Krutchinsky AN, Zhang WZ, Chait BT, Matunis MJ (2002) Proteomic analysis of the mammalian nuclear pore complex. J Cell Biol 158:915–927
D’Angelo MA, Raices M, Panowski SH, Hetzer MW (2009) Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell 136:284–295
de Lichtenberg U, Jensen LJ, Brunak S, Bork P (2005) Dynamic complex formation during the yeast cell cycle. Science 307:724–727
Fabre E, Hurt E (1997) Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking. Annu Rev Genet 31:277–313
Finan K, Raulf A, Heilemann M (2015) A set of homo-oligomeric standards allows accurate protein counting. Angew Chem Int Ed 54:12049–12052
Franke WW (1966) Isolated nuclear membranes. J Cell Biol 31:619–623
Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, O’Shea EK, Weissman JS (2003) Global analysis of protein expression in yeast. Nature 425:737–741
Griffis ER, Altan N, Lippincott-Schwartz J, Powers MA (2002) Nup98 is a mobile nucleoporin with transcription-dependent dynamics. Mol Biol Cell 13:1282–1297
Hinshaw JE, Milligan RA (2003) Nuclear pore complexes exceeding eightfold rotational symmetry. J Struct Biol 141:259–268
Huh WK, Falvo JV, Gerke LC, Carroll AS, Howson RW, Weissman JS, O'Shea EK (2003) Global analysis of protein localization in budding yeast. Nature 425:686–691
Kopek BG, Shtengel G, Xu CS, Clayton DA, Hess HF (2012) Correlative 3D superresolution fluorescence and electron microscopy reveal the relationship of mitochondrial nucleoids to membranes. Proc Natl Acad Sci U S A 109:6136–6141
Löschberger A, Svd L, Dabauvalle M-C, Rieger B, Heilemann M, Krohne G, Sauer M (2012) Super-resolution imaging visualizes the eightfold symmetry of gp210 proteins around the nuclear pore complex and resolves the central channel with nanometer resolution. J Cell Sci 125:570–575
Loschberger A, Franke C, Krohne G, van de Linde S, Sauer M (2014) Correlative super-resolution fluorescence and electron microscopy of the nuclear pore complex with molecular resolution. J Cell Sci 127:4351–4355
Ma J, Yang W (2010) Three-dimensional distribution of transient interactions in the nuclear pore complex obtained from single-molecule snapshots. Proc Natl Acad Sci USA 107:7305–7310
Mi L, Goryaynov A, Lindquist A, Rexach M, Yang WD (2015) Quantifying nucleoporin stoichiometry inside single nuclear pore complexes in vivo. Sci Rep 5:9372
Nanguneri S, Flottmann B, Horstmann H, Heilemann M, Kuner T (2012) Three-dimensional, tomographic super-resolution fluorescence imaging of serially sectioned thick samples. Plos One 7:e38098
Ori A, Banterle N, Iskar M, Andrés-Pons A, Escher C, Khanh Bui H, Sparks L, Solis-Mezarino V, Rinner O, Bork P et al (2013) Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines. Mol Syst Biol 9:648
Pouwels LJ, Zhang L, Chan NH, Dorrestein PC, Wachter RM (2008) Kinetic isotope effect studies on the de novo rate of chromophore formation in fast- and slow-maturing GFP variants. Biochemistry 47:10111–10122
Rabut G, Doye V, Ellenberg J (2004) Mapping the dynamic organization of the nuclear pore complex inside single living cells. Nat Cell Biol 6:1114–1121
Reichelt R, Holzenburg A, Buhle EL, Jarnik M, Engel A, Aebi U (1990) Correlation between structure and mass-distribution of the nuclear-pore complex and of distinct pore complex components. J Cell Biol 110:883–894
Rout MP, Blobel G (1993) Isolation of the yeast nuclear pore complex. J Cell Biol 123:771–783
Rout MP, Aitchison JD, Suprapto A, Hjertaas K, Zhao Y, Chait BT (2000) The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol 148:635–651
Savas JN, Toyama BH, Xu T, Yates JR, Hetzer MW (2012) Extremely long-lived nuclear pore proteins in the rat brain. Science 335:942–942
Strambio-De-Castillia C, Niepel M, Rout MP (2010) The nuclear pore complex: bridging nuclear transport and gene regulation. Nature Reviews Molecular Cell Biology 11:490–501
Stuwe T, Correia AR, Lin DH, Paduch M, Lu VT, Kossiakoff AA, Hoelz A (2015) Architecture of the nuclear pore complex coat. Science 347:1148–1152
Suntharalingam M, Wente SR (2003) Peering through the pore: nuclear pore complex structure, assembly, and function. Developmental Cell 4:775–789
Szymborska A, de Marco A, Daigle N, Cordes VC, Briggs JAG, Ellenberg J (2013) Nuclear pore scaffold structure analyzed by super-resolution microscopy and particle averaging. Science 341:655–658
Tanudji M, Hevi S, Chuck SL (2002) Improperly folded green fluorescent protein is secreted via a non-classical pathway. J Cell Sci 115:3849–3857
Tie HC, Madugula V, Lu L (2016) The development of a single molecule fluorescence standard and its application in estimating the stoichiometry of the nuclear pore complex. Biochem Biophys Res Commun 478:1694–1699
von Appen A, Beck M (2016) Structure determination of the nuclear pore complex with three-dimensional cryo electron microscopy. J Mol Biol 428:2001–2010
von Appen A, Kosinski J, Sparks L, Ori A, DiGuilio AL, Vollmer B, Mackmull MT, Banterle N, Parca L, Kastritis P et al (2015) In situ structural analysis of the human nuclear pore complex. Nature 526:140
Wente SR, Blobel G (1994) Nup145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear-envelope structure. Journal Of Cell Biology 125:955–969
Yang Q, Rout MP, Akey CW (1998) Three-dimensional architecture of the Isolated yeast nuclear pore complex: functional and evolutionary implications. Mol Cell 1:223–234
Acknowledgments
This work is supported by National Natural Science Foundation of China (61575046, 11574056, and 31500599) and Science and Technology Commission of Shanghai Municipality (Shanghai Rising-Star Program, 16QA1400400).
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Mi, L., Yao, L., Ma, J. (2018). Structure of Yeast Nuclear Pore Complexes. In: Yang, W. (eds) Nuclear-Cytoplasmic Transport. Nucleic Acids and Molecular Biology, vol 33. Springer, Cham. https://doi.org/10.1007/978-3-319-77309-4_2
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DOI: https://doi.org/10.1007/978-3-319-77309-4_2
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