Facilitated aggregation of FG nucleoporins under molecular crowding conditions

EMBO Reports

Volumn 14, Issue 2, 2013, Pages 178-183

  Milles, Sigrid ^a   Huy Bui, Khanh ^a   Koehler, Christine ^a   Eltsov, Mikhail ^a   Beck, Martin ^a   Lemke, Edward A ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

amyloid fibres; electron microscopy; fluorescence spectroscopy; intrinsically disordered protein; nuclear pore complex

Indexed keywords

AMYLOID; CARRIER PROTEIN; GLYCINE; NUCLEAR TRANSPORT PROTEIN; NUCLEOPORIN; PHENYLALANINE; UNCLASSIFIED DRUG;

ARTICLE; BETA SHEET; ELECTRON MICROSCOPY; FLUORESCENCE SPECTROSCOPY; HUMAN; HYDROGEL; MOLECULAR CROWDING; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR PORE COMPLEX; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; SUPRAMOLECULAR CHEMISTRY; ULTRASTRUCTURE; YEAST;

AMYLOID; BETA KARYOPHERINS; DEXTRANS; HUMANS; HYDROGELS; KINETICS; NUCLEAR PORE COMPLEX PROTEINS; OSMOLAR CONCENTRATION; POROSITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84873414227     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/embor.2012.204     Document Type: Article

References (36)

1. D'Angelo MA, Hetzer MW (2008) Structure, dynamics and function of nuclear pore complexes. Trends Cell Biol 18: 456-466
2. Elad N, Maimon T, Frenkiel-Krispin D, Lim RY, Medalia O (2009) Structural analysis of the nuclear pore complex by integrated approaches. Curr Opin Struct Biol 19: 226-232
3. Beck M, Lucic V, Forster F, Baumeister W, Medalia O (2007) Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature 449: 611-615
4. Maimon T, Elad N, Dahan I, Medalia O (2012) The human nuclear pore complex as revealed by cryo-electron tomography. Structure 20: 998-1006
5. Nehrbass U, Kern H, Mutvei A, Horstmann H, Marshallsay B, Hurt EC (1990) Nsp1-a yeast nuclear-envelope protein localized at the nuclear-pores exerts its essential function by its carboxy-terminal domain. Cell 61: 979-989
6. Frey S, Gorlich D (2007) A saturated FG-repeat hydrogel can reproduce the permeability propertiesofnuclear porecomplexes. Cell 130: 512-523
7. Yamada J etal (2010) A bimodal distribution of twodistinctcategories of intrinsically disordered structures with separate functions in FG nucleoporins. Mol Cell Proteomics 9: 2205-2224
8. Terry LJ, Wente SR (2009) Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport. Eukaryot Cell 8: 1814-1827
9. Denning DP, Patel SS, Uversky V, Fink AL, Rexach M (2003) Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc Natl Acad Sci USA 100: 2450-2455
10. Lim RY, Huang NP, Koser J, Deng J, Lau KH, Schwarz-Herion K, Fahrenkrog B, Aebi U (2006) Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport. Proc Natl Acad Sci USA 103: 9512-9517
11. Lim RY, Fahrenkrog B, Koser J, Schwarz-Herion K, Deng J, Aebi U (2007) Nanomechanical basis of selective gating by the nuclear pore complex. Science 318: 640-643
12. Frey S, Richter RP, Gorlich D (2006) FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science314: 815-817
13. Milles S, Lemke EA (2011) Single molecule study of the intrinsically disordered FG-repeat nucleoporin 153. Biophys J101: 1710-1719
14. Halfmann R, Wright J, Alberti S, Lindquist S, Rexach M (2012) Prion formation by a yeast GLFG nucleoporin. Prion 6: 391-399
15. Alberti S, Halfmann R, King O, Kapila A, Lindquist S (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell137: 146-158
16. Frey S, Gorlich D (2009) FG/Fx FG as well as GLFG repeats form a selective permeability barrier with self-healing properties. EMBOJ 28: 2554-2567
17. Hulsmann BB, Labokha AA, Gorlich D (2012) The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model. Cell150: 738-751
18. Mohr D, Frey S, Fischer T, Guttler T, Gorlich D (2009) Characterisation of the passive permeability barrier of nuclear pore complexes. EMBOJ 28: 2541-2553
19. Ader C, Frey S, Maas W, Schmidt HB, Gorlich D, Baldus M (2010) Amyloid-like interactions within nucleoporin FG hydrogels. Proc Natl Acad Sci USA 107: 6281-6285
20. Petri M, Frey S, Menzel A, Goerlich D, Techert SA (2012) Structural characterization of nanoscale meshworks within a nucleoporin FG hydrogel. Biomacromolecules 13: 1882-1889
21. Mukhopadhyay S, Krishnan R, Lemke EA, Lindquist S, Deniz AA (2007) A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc Natl Acad Sci USA 104: 2649-2654
22. Jain N, Bhattacharya M, Mukhopadhyay S (2011) Chain collapse of an amyloidogenic intrinsically disordered protein. Biophys J 101: 1720-1729
23. Tompa P (2009) Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins. Febs J276: 5406-5415
24. Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333-366
25. Vassar PS, Culling CF (1959) Fluorescent stains, with special reference to amyloid and connective tissues. Arch Pathol 68: 487-498
26. Krishnan R, Goodman JL, Mukhopadhyay S, Pacheco CD, Lemke EA, Deniz AA, Lindquist S (2012) Conserved features of intermediates in amyloid assembly determine their benign or toxic states. Proc Natl Acad Sci USA 109: 11172-11177
27. Sachse C, Grigorieff N, Fandrich M (2010) Nanoscale flexibility parameters of Alzheimer amyloid fibrils determined by electron cryo-microscopy. Angew Chem Int Ed Engl 49: 1321-1323
28. Alber F et al (2007) The molecular architecture of the nuclear pore complex. Nature 450: 695-701
29. Zhou HX, Rivas G, Minton AP (2008) Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences. Annu Rev Biophys 37: 375-397
30. Peters R (2009) Functionalization of a nanopore: the nuclear pore complex paradigm. Biochim Biophys Acta 1793: 1533-1539
31. 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
32. Colletier JP etal (2011) Molecular basis for amyloid-beta polymorphism. Proc Natl Acad Sci USA 108: 16938-16943
33. Miller MW, Caracciolo MR, Berlin WK, Hanover JA (1999) Phosphorylation and glycosylation of nucleoporins. Arch Biochem Biophys367: 51-60
34. Yang Z, Liang G, Wang L, Xu B (2006) Using a kinase/phosphatase switch to regulate a supramolecular hydrogel and forming the supramolecular hydrogel in vivo. JAm Chem Soc 128: 3038-3043
35. Gao Y, Yang Z, Kuang Y, Ma ML, Li J, Zhao F, Xu B (2010) Enzyme-instructed self-assembly of peptide derivatives to form nanofibers and hydrogels. Biopolymers94: 19-31
36. Milles S, Tyagi S, Banterle N, Koehler C, Van Delinder V, Plass T, Neal AP, Lemke EA (2012) Click strategies for single-molecule protein fluorescence. J Am Chem Soc 134: 5187-5195