Visualization of Transient Protein-Protein Interactions that Promote or Inhibit Amyloid Assembly

Molecular Cell

Volumn 55, Issue 2, 2014, Pages 214-226

  Karamanos, Theodoros K ^a   Kalverda, Arnout P ^a   Thompson, Gary S ^a   Radford, Sheena E ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; DIMER;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

AMINO ACID SUBSTITUTION; AMYLOID; ANIMALS; BETA 2-MICROGLOBULIN; BINDING SITES; HUMANS; KINETICS; MICE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN INTERACTION MAPPING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING;

EID: 84904559289     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2014.05.026     Document Type: Article

References (51)

1. Aguzzi A., Sigurdson C., Heikenwaelder M. Molecular mechanisms of prion pathogenesis. Annu. Rev. Pathol. 2008, 3:11-40.
2. Bae S.-H., Legname G., Serban A., Prusiner S.B., Wright P.E., Dyson H.J. Prion proteins with pathogenic and protective mutations show similar structure and dynamics. Biochemistry 2009, 48:8120-8128.
3. Baker N.A., Sept D., Joseph S., Holst M.J., McCammon J.A. Electrostatics of nanosystems: Application to microtubules and the ribosome. Proc. Natl. Acad. Sci. USA 2001, 98:10037-10041.
4. Balch W.E., Morimoto R.I., Dillin A., Kelly J.W. Adapting proteostasis for disease intervention. Science 2008, 319:916-919.
5. Baskakov I.V. The many shades of prion strain adaptation. Prion 2014, Published online February 11, 2014. 10.4161/pri.27836.
6. Brundin P., Melki R., Kopito R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat. Rev. Mol. Cell Biol. 2010, 11:301-307.
7. Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M.C., Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002, 416:507-511.
8. Bunka D.H.J., Mantle B.J., Morten I.J., Tennent G.A., Radford S.E., Stockley P.G. Production and characterization of RNA aptamers specificfor amyloid fibril epitopes. J. Biol. Chem. 2007, 282:34500-34509.
9. Calabrese M.F., Miranker A.D. Metal binding sheds light on mechanisms of amyloid assembly. Prion 2009, 3:1-4.
10. Campioni S., Mannini B., Zampagni M., Pensalfini A., Parrini C., Evangelisti E., Relini A., Stefani M., Dobson C.M., Cecchi C., Chiti F. A causative link between the structure of aberrant protein oligomers and their toxicity. Nat. Chem. Biol. 2010, 6:140-147.
11. Chien P., Weissman J.S. Conformational diversity in a yeast prion dictates its seeding specificity. Nature 2001, 410:223-227.
12. Chien P., DePace A.H., Collins S.R., Weissman J.S. Generation of prion transmission barriers by mutational control of amyloid conformations. Nature 2003, 424:948-951.
13. Chien P., Weissman J.S., DePace A.H. Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem. 2004, 73:617-656.
14. Chiti F., Dobson C.M. Amyloid formation by globular proteins under native conditions. Nat. Chem. Biol. 2009, 5:15-22.
15. Clore G.M., Iwahara J. Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes. Chem. Rev. 2009, 109:4108-4139.
16. Cremades N., Cohen S.I.A., Deas E., Abramov A.Y., Chen A.Y., Orte A., Sandal M., Clarke R.W., Dunne P., Aprile F.A., et al. Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell 2012, 149:1048-1059.
17. Dumoulin M., Last A.M., Desmyter A., Decanniere K., Canet D., Larsson G., Spencer A., Archer D.B., Sasse J., Muyldermans S., et al. A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Nature 2003, 424:783-788.
18. 2-microglobulin amyloid assembly at neutral pH involving a specific proline switch. J.Mol. Biol. 2009, 386:1312-1326.
19. 2-microglobulin amyloid assembly. FEBS J. 2011, 278:3868-3883.
20. Eichner T., Kalverda A.P., Thompson G.S., Homans S.W., Radford S.E. Conformational conversion during amyloid formation at atomic resolution. Mol. Cell 2011, 41:161-172.
21. Eisenberg D., Jucker M. The amyloid state of proteins in human diseases. Cell 2012, 148:1188-1203.
22. 2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci. 2000, 9:831-845.
23. Fitzpatrick A.W.P., Debelouchina G.T., Bayro M.J., Clare D.K., Caporini M.A., Bajaj V.S., Jaroniec C.P., Wang L., Ladizhansky V., Müller S.A., et al. Atomic structure and hierarchical assembly of a cross-β amyloid fibril. Proc. Natl. Acad. Sci. USA 2013, 110:5468-5473.
24. 2-microglobulin. Biochem. Biophys. Res. Commun. 1985, 129:701-706.
25. Giasson B.I., Forman M.S., Higuchi M., Golbe L.I., Graves C.L., Kotzbauer P.T., Trojanowski J.Q., Lee V.M.Y. Initiation and synergistic fibrillization of tau and α-synuclein. Science 2003, 300:636-640.
26. Greenwald J., Riek R. Biology of amyloid: structure, function, and regulation. Structure 2010, 18:1244-1260.
27. Greenwald J., Buhtz C., Ritter C., Kwiatkowski W., Choe S., Maddelein M.-L., Ness F., Cescau S., Soragni A., Leitz D. The mechanism of prion inhibition by HET-S. Mol. Cell 2010, 38:889-899.
28. Guo J.L., Covell D.J., Daniels J.P., Iba M., Stieber A., Zhang B., Riddle D.M., Kwong L.K., Xu Y., Trojanowski J.Q., Lee V.M. Distinct α-synuclein strains differentially promote tau inclusions in neurons. Cell 2013, 154:103-117.
29. 2-microglobulin upon release from the MHC-1. J.Am. Soc. Mass Spectrom. 2009, 20:278-286.
30. Hoyer W., Grönwall C., Jonsson A., Ståhl S., Härd T. Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation. Proc. Natl. Acad. Sci. USA 2008, 105:5099-5104.
31. 2-microglobulin suggests a molecular model for the fibril. Proc. Natl. Acad. Sci. USA 2004, 101:10584-10589.
32. 1H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule. J.Am. Chem. Soc. 2004, 126:5879-5896.
33. Jahn T.R., Parker M.J., Homans S.W., Radford S.E. Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat. Struct. Mol. Biol. 2006, 13:195-201.
34. Maji S.K., Perrin M.H., Sawaya M.R., Jessberger S., Vadodaria K., Rissman R.A., Singru P.S., Nilsson K.P., Simon R., Schubert D., et al. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 2009, 325:328-332.
35. Middleton C.T., Marek P., Cao P., Chiu C.-C., Singh S., Woys A.M., de Pablo J.J., Raleigh D.P., Zanni M.T. Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor. Nat. Chem. 2012, 4:355-360.
36. Neudecker P., Robustelli P., Cavalli A., Walsh P., Lundström P., Zarrine-Afsar A., Sharpe S., Vendruscolo M., Kay L.E. Structure of an intermediate state in protein folding and aggregation. Science 2012, 336:362-366.
37. Otzen D. Functional amyloid: turning swords into plowshares. Prion 2010, 4:256-264.
38. 2-microglobulin studied by NMR. J.Mol. Biol. 2005, 346:279-294.
39. 2-microglobulin: kinetics, thermodynamics, and structure. J.Mol. Biol. 2013, 425:2722-2736.
40. Rudolph M.G., Shen L.Q., Lamontagne S.A., Luz J.G., Delaney J.R., Ge Q., Cho B.K., Palliser D., McKinley C.A., Chen J., et al. A peptide that antagonizes TCR-mediated reactions with both syngeneic and allogeneic agonists: functional and structural aspects. J.Immunol. 2004, 172:2994-3002.
41. 2-microglobulin studied by mutational analysis. J.Mol. Biol. 2008, 382:1242-1255.
42. Sarell C.J., Stockley P.G., Radford S.E. Assessing the causes and consequences of co-polymerization in amyloid formation. Prion 2013, 7:359-368.
43. Sarell C.J., Woods L.A., Su Y., Debelouchina G.T., Ashcroft A.E., Griffin R.G., Stockley P.G., Radford S.E. Expanding the repertoire of amyloid polymorphs by co-polymerization of related protein precursors. J.Biol. Chem. 2013, 288:7327-7337.
44. Schanda P., Kupče E., Brutscher B. SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds. J.Biomol. NMR 2005, 33:199-211.
45. Sindi S.S., Serio T.R. Prion dynamics and the quest for the genetic determinant in protein-only inheritance. Curr. Opin. Microbiol. 2009, 12:623-630.
46. 2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry. Proc. Natl. Acad. Sci. USA 2010, 107:6794-6798.
47. Tang C., Iwahara J., Clore G.M. Visualization of transient encounter complexes in protein-protein association. Nature 2006, 444:383-386.
48. Tang C., Ghirlando R., Clore G.M. Visualization of transient ultra-weak protein self-association in solution using paramagnetic relaxation enhancement. J.Am. Chem. Soc. 2008, 130:4048-4056.
49. +]. Nat. Struct. Mol. Biol. 2009, 16:598-605.
50. Xue W.F., Homans S.W., Radford S.E. Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc. Natl. Acad. Sci. USA 2008, 105:8926-8931.
51. Zhuravleva A., Gierasch L.M. Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proc. Natl. Acad. Sci. USA 2011, 108:6987-6992.