Intrinsically unstructured proteins and neurodegenerative diseases: Conformational promiscuity at its best

IUBMB Life

Volumn 63, Issue 7, 2011, Pages 478-488

  Das, Samir ^a   Mukhopadhyay, Debashis ^a  

^a SAHA INSTITUTE OF NUCLEAR PHYSICS   (India)

Author keywords

Alzheimer's disease; conformational switch; Huntington's disease; IUP; neurodegenerative diseases; Parkinson's disease

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID PRECURSOR PROTEIN; AMYLOID PRECURSOR PROTEIN INTRACELLULAR C TERMINAL DOMAIN; HUNTINGTIN; INTRINSICALLY UNSTRUCTURED PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; DEGENERATIVE DISEASE; HUMAN; HUNTINGTON CHOREA; INFORMATION PROCESSING; NERVE CELL NETWORK; NONHUMAN; PARKINSON DISEASE; PHENOTYPE; PHOSPHORYLATION; PREVALENCE; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN HOMEOSTASIS; PROTEIN MISFOLDING; PROTEIN STRUCTURE; REVIEW; SIGNAL TRANSDUCTION;

HUMANS; MODELS, MOLECULAR; NEURODEGENERATIVE DISEASES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEINS;

EID: 79959621499     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.498     Document Type: Review

References (53)

1. Uversky, V. N., (2011) Flexible nets of malleable guardians: intrinsically disordered chaperones in neurodegenerative diseases. Chem. Rev. 111, 1134-1166
2. Lansbury, P. T., and, Lashuel, H. A., (2006) A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 443, 774-779. (Pubitemid 44622681)
3. Ross, C. A., and, Poirier, M. A., (2004) Protein aggregation and neurodegenerative disease. Nat. Med. 10, S10-S17. (Pubitemid 38901862)
4. Wright, P. E., and, Dyson, H. J., (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321-331. (Pubitemid 29516173)
5. Uversky, V. N., (2002) What does it mean to be natively unfolded? Eur. J. Biochem. 269, 2-12. (Pubitemid 34107333)
6. He, B., Wang, K., Liu, Y., Xue, B., Uversky, V. N., et al. (2009) Predicting intrinsic disorder in proteins: an overview. Cell. Res. 19, 929-949.
7. Tompa, P., Szasz, C., and, Buday, L., (2005) Structural disorder throws new light on moonlighting. Trends Biochem. Sci. 30, 484-489. (Pubitemid 41206503)
8. Fink, A. L., (2005) Natively unfolded proteins. Curr. Opin. Struct. Biol. 15, 35-41. (Pubitemid 40249507)
9. Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., et al. (2001) Intrinsically disordered protein. J. Mol. Graph Model. 19, 26-59. (Pubitemid 32411501)
10. Jeffery, C. J., (1999) Moonlighting proteins. Trends Biochem. Sci. 24, 8-11. (Pubitemid 29074455)
11. Tompa, P., (2003) Intrinsically unstructured proteins evolve by repeat expansion. Bioessays 25, 847-855. (Pubitemid 37081750)
12. Tompa, P., (2005) The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 579, 3346-3354. (Pubitemid 40804685)
13. Gunasekaran, K., Tsai, C. J., Kumar, S., Zanuy, D., and, Nussinov, R., (2003) Extended disordered proteins: targeting function with less scaffold. Trends Biochem. Sci. 28, 81-85. (Pubitemid 36165136)
14. Gsponer, J., Futschik, M. E., Teichmann, S. A., and, Babu, M. M., (2008) Tight regulation of unstructured proteins: from transcript synthesis to protein degradation. Science 322, 1365-1368. (Pubitemid 352775246)
15. Huberts, D. H., and, van der Klei, I. J., (2010) (2010) Moonlighting proteins: an intriguing mode of multitasking. Biochim. Biophys. Acta 1803, 520-525.
16. Shimizu, K., and, Toh, H., (2009) Interaction between intrinsically disordered proteins frequently occurs in a human protein-protein interaction network. J. Mol. Biol. 392, 1253-1265.
17. Vavouri, T., Semple, J. I., Garcia-Verdugo, R., and, Lehner, B., (2009) Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity. Cell 138, 198-208.
18. Tsvetkov, P., Reuven, N., and, Shaul, Y., Ubiquitin-independent p53 proteasomal degradation. Cell Death Differ. 17, 103-108.
19. Raychaudhuri, S., Dey, S., Bhattacharyya, N. P., and, Mukhopadhyay, D., (2009) The role of intrinsically unstructured proteins in neurodegenerative diseases. PLoS One 4, e5566.
20. Prilusky, J., Felder, C., Zeev-Ben-Mordehai, T., Rydberg, E., Man, O., et al. (2005) FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 21, 3435-3438. (Pubitemid 41222454)
21. Agorogiannis, E. I., Agorogiannis, G. I., Papadimitriou, A., and, Hadjigeorgiou, G. M., (2004) Protein misfolding in neurodegenerative diseases. Neuropathol. Appl. Neurobiol. 30, 215-224. (Pubitemid 38789243)
22. Hague, S. M., Klaffke, S., and, Bandmann, O., (2005) Neurodegenerative disorders: Parkinson's disease and Huntington's disease. J. Neurol. Neurosurg. Psychiatr. 76, 1058-1063. (Pubitemid 41081275)
23. Williamson, T. E., Vitalis, A., Crick, S. L., and, Pappu, R. V., (2010) Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin. J. Mol. Biol. 396, 1295-1309.
24. Kim, M. W., Chelliah, Y., Kim, S. W., Otwinowski, Z., and, Bezprozvanny, I., (2009) Secondary structure of Huntingtin amino-terminal region. Structure 17, 1205-1212.
25. Ekman, D., and, Elofsson, A., (2010) Identifying and quantifying orphan protein sequences in fungi. J. Mol. Biol. 396, 396-405.
26. Munishkina, L. A., Phelan, C., Uversky, V. N., and, Fink, A. L., (2003) Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes. Biochemistry 42, 2720-2730. (Pubitemid 36330626)
27. Kim, S., Seo, J. H., and, Suh, Y. H., (2004) Alpha-synuclein, Parkinson's disease, and Alzheimer's disease. Parkinsonism Relat. Disord. 10 (Suppl 1), S9-S13.
28. Uversky, V. N., (2003) A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders. J. Biomol. Struct. Dyn. 21, 211-234. (Pubitemid 37204199)
29. Eliezer, D., Kutluay, E., Bussell, R., Jr., and, Browne, G., (2001) Conformational properties of alpha-synuclein in its free and lipid-associated states. J. Mol. Biol. 307, 1061-1073. (Pubitemid 33029953)
30. Bussell, R., Jr., and, Eliezer, D., (2003) A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins. J. Mol. Biol. 329, 763-778. (Pubitemid 36629369)
31. de Laureto, P. P., Tosatto, L., Frare, E., Marin, O., Uversky, V. N., et al. (2006) Conformational properties of the SDS-bound state of alpha-synuclein probed by limited proteolysis: unexpected rigidity of the acidic C-terminal tail. Biochemistry 45, 11523-11531. (Pubitemid 44454000)
32. Murray, I. V., Giasson, B. I., Quinn, S. M., Koppaka, V., Axelsen, P. H., et al. (2003) Role of alpha-synuclein carboxy-terminus on fibril formation in vitro. Biochemistry 42, 8530-8540. (Pubitemid 36875420)
33. Uversky, V. N., Li, J., and, Fink, A. L., (2001) Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J. Biol. Chem. 276, 10737-10744. (Pubitemid 38089246)
34. Hardy, J., and, Selkoe, D. J., (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356. (Pubitemid 34790756)
35. Mattson, M. P., (2004) Pathways towards and away from Alzheimer's disease. Nature 430, 631-639. (Pubitemid 39061671)
36. Raychaudhuri, M., and, Mukhopadhyay, D., (2007) AICD and its adaptors-in search of new players. J. Alzheimers Dis. 11, 343-358. (Pubitemid 47096601)
37. Ghosal, K., Vogt, D. L., Liang, M., Shen, Y., Lamb, B. T., et al. (2009) Alzheimer's disease-like pathological features in transgenic mice expressing the APP intracellular domain. Proc. Natl. Acad. Sci. USA 106, 18367-18372.
38. Ramelot, T. A., Gentile, L. N., and, Nicholson, L. K., (2000) Transient structure of the amyloid precursor protein cytoplasmic tail indicates preordering of structure for binding to cytosolic factors. Biochemistry 39, 2714-2725. (Pubitemid 30148926)
39. Iakoucheva, L. M., Radivojac, P., Brown, C. J., O'Connor, T. R., Sikes, J. G., et al. (2004) The importance of intrinsic disorder for protein phosphorylation. Nucleic Acids Res. 32, 1037-1049. (Pubitemid 38854704)
40. Russo, C., Dolcini, V., Salis, S., Venezia, V., Zambrano, N., et al. (2002) Signal transduction through tyrosine-phosphorylated C-terminal fragments of amyloid precursor protein via an enhanced interaction with Shc/Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain. J. Biol. Chem. 277, 35282-35288.
41. Zhou, D., Noviello, C., D'Ambrosio, C., Scaloni, A., and, D'Adamio, L., (2004) Growth factor receptor-bound protein 2 interaction with the tyrosine-phosphorylated tail of amyloid beta precursor protein is mediated by its Src homology 2 domain. J. Biol. Chem. 279, 25374-25380. (Pubitemid 38756794)
42. Raychaudhuri, M., and, Mukhopadhyay, D., (2010) Grb2-mediated alteration in the trafficking of AbetaPP: insights from Grb2-AICD interaction. J. Alzheimers Dis. 20, 275-292.
43. Tamayev, R., Zhou, D., and, D'Adamio, L., (2009) The interactome of the amyloid beta precursor protein family members is shaped by phosphorylation of their intracellular domains. Mol. Neurodegener. 4, 28.
44. Radzimanowski, J., Ravaud, S., Schlesinger, S., Koch, J., Beyreuther, K., et al. (2008) Crystal structure of the human Fe65-PTB1 domain. J. Biol. Chem. 283, 23113-23120.
45. DeLano, W. L., (2002) The PyMOL Molecular Graphics System. Available at:. Accessed on February 2011.
46. Nicholls, A., Sharp, K. A., and, Honig, B., (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
47. Ogura, K., Tsuchiya, S., Terasawa, H., Yusawa, S., Hatanaka, H., et al. (1999) Solution structure of the SH2 domain of Grb2 complexed with the Shc-derived phosphotyrosine-containing peptide. J.Mol. Biol. 289, 439-445. (Pubitemid 29295115)
48. Zhou, M. M., Meadows, R. P., Logan, T. M., Yoon, H. S., Wade, W. S., et al. (1995) Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor. Proc. Natl. Acad. Sci. USA 92, 7784-7788.
49. Zhang, Z., Lee, C. H., Mandiyan, V., Borg, J. P., Margolis, B., et al. (1997) Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain. EMBO J. 16, 6141-6150. (Pubitemid 27458334)
50. Ramelot, T. A., and, Nicholson, L. K., (2001) Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR. J. Mol. Biol. 307, 871-884. (Pubitemid 33027665)
51. Rahuel, J., Gay, B., Erdmann, D., Strauss, A., Garcia-Echeverría, C., et al. (1996) Structural basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode. Nat. Struct. Biol. 3, 586-589.
52. Liu, Y., and, Kulesz-Martin, M., (2001) p53 protein at the hub of cellular DNA damage response pathways through sequence-specific and non-sequence-specific DNA binding. Carcinogenesis 22, 851-860. (Pubitemid 32514948)
53. Chi, E. Y., Krishnan, S., Randolph, T. W., and, Carpenter, J. F., (2003) Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation. Pharm. Res. 20, 1325-1336. (Pubitemid 37164039)