Unusual biophysics of immune signaling-related intrinsically disordered proteins

Self/Nonself - Immune Recognition and Signaling

Volumn 1, Issue 4, 2010, Pages 271-281

  Sigalov, Alexander B ^a  

^a SignaBlok Inc   (United States)

Author keywords

B cell receptor; Circular dichroism; Cytoplasmic domains; Disorder to order transition; Fc receptors; Folding; Homooligomerization; Immune signaling; Intrinsically disordered proteins; NMR; Nuclear magnetic resonance; Protein folding; Protein oligomerization; Protein lipid interactions; Protein protein interactions; Receptor signaling; Signal transduction; T cell receptor

Indexed keywords

CD3 DELTA PROTEIN; CD3 EPSILON PROTEIN; CD3 GAMMA PROTEIN; CD79A ANTIGEN; CD79B ANTIGEN; FC RECEPTOR GAMMA PROTEIN; INTRINSICALLY DISORDERED PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CYTOPLASM; DIMERIZATION; GEL FILTRATION; HUMAN; MEMBRANE BINDING; MEMBRANE MODEL; MOLECULAR MECHANICS; MOLECULAR WEIGHT; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION;

EID: 79851492077     PISSN: 19382030     EISSN: 19382049     Source Type: Journal    
DOI: 10.4161/self.1.4.13641     Document Type: Article

References (57)

1. Sigalov AB. Multichain immune recognition receptor signaling: different players, same game? Trends Immunol 2004; 25:583-9.
2. Sigalov AB. New therapeutic strategies targeting transmembrane signal transduction in the immune system. Cell Adh Migr 2010; 4:255-67.
3. Sigalov AB. The SCHOOL of nature. I. Transmembrane signaling. Self/Nonself-Immune Recognition and Signaling 2010; 1:4-39.
4. Sigalov A, Aivazian D, Stern L. Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. Biochemistry 2004; 43:2049-61.
5. Sigalov AB, Aivazian DA, Uversky VN, Stern LJ. Lipid-binding activity of intrinsically unstructured cytoplasmic domains of multichain immune recognition receptor signaling subunits. Biochemistry 2006; 45:15731-9.
6. Aivazian DA, Stern LJ. Phosphorylation of T cell receptor zeta is regulated by a lipid dependent folding transition. Nat Struct Biol 2000; 7:1023-6.
7. Skerrett RJ. Analysis of the reversible aggregation of macromolecules in a centrifugal field. J Chem Soc, Faraday Trans 1972; 68:1328-38.
8. Uversky VN. Amyloidogenesis of natively unfolded proteins. Curr Alzheimer Res 2008; 5:260-87.
9. Sigalov AB. Immune cell signaling: a novel mechanistic model reveals new therapeutic targets. Trends Pharmacol Sci 2006; 27:518-24.
10. Sigalov AB. The SCHOOL of nature. II. Protein order, disorder and oligomericity in transmembrane signaling. Self/Nonself-Immune Recognition and Signaling 2010; 1:89-102.
11. Singh VK, Pacheco I, Uversky VN, Smith SP, MacLeod RJ, Jia Z. Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress. J Mol Biol 2008; 380:313-26.
12. Danielsson J, Liljedahl L, Barany-Wallje E, Sonderby P, Kristensen LH, Martinez-Yamout MA, et al. The intrinsically disordered RNR inhibitor Sml1 is a dynamic dimer. Biochemistry 2008; 47:13428-37.
13. Lanza DC, Silva JC, Assmann EM, Quaresma AJ, Bressan GC, Torriani IL, et al. Human FEZ1 has characteristics of a natively unfolded protein and dimerizes in solution. Proteins 2009; 74:104-21.
14. Simon SM, Sousa FJ, Mohana-Borges R, Walker GC. Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products. Proc Natl Acad Sci USA 2008; 105:1152-7.
15. Sigalov AB, Hendricks GM. Membrane binding mode of intrinsically disordered cytoplasmic domains of T cell receptor signaling subunits depends on lipid composition. Biochem Biophys Res Commun 2009; 389:388-93.
16. Sigalov AB, Kim WM, Saline M, Stern LJ. The intrinsically disordered cytoplasmic domain of the T cell receptor zeta chain binds to the nef protein of simian immunodeficiency virus without a disorder-to-order transition. Biochemistry 2008; 47:12942-4.
17. Sigalov AB, Zhuravleva AV, Orekhov VY. Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Biochimie 2007; 89:419-21.
18. Berko D, Carmi Y, Cafri G, Ben-Zaken S, Sheikhet HM, Tzehoval E, et al. Membrane-anchored beta 2-microglobulin stabilizes a highly receptive state of MHC class I molecules. J Immunol 2005; 174:2116-23.
19. Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, et al. Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. Nature 2002; 415:549-53.
20. Sigalov AB. SCHOOL model and new targeting strategies. Adv Exp Med Biol 2008; 640:268-311.
21. Sigalov AB. The SCHOOL of nature. III. From mechanistic understanding to novel therapies. Self/Nonself-Immune Recognition and Signaling 2010; 3:192-224.
22. Clark AJ, Petty HR. A cell permeant peptide containing the cytoplasmic tail sequence of Fc receptor type IIA reduces calcium signaling and phagolysosome formation in neutrophils. Cell Immunol 2010; 261:153-8.
23. Metallo SJ. Intrinsically disordered proteins are potential drug targets. Curr Opin Chem Biol 2010; 14:481-8.
24. Tompa P, Fuxreiter M. Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem Sci 2008; 33:2-8.
25. Mittag T, Kay LE, Forman-Kay JD. Protein dynamics and conformational disorder in molecular recognition. J Mol Recognit 2010; 23:105-16.
26. Clark MR, Campbell KS, Kazlauskas A, Johnson SA, Hertz M, Potter TA, et al. The B cell antigen receptor complex: association of Igalpha and Igbeta with distinct cytoplasmic effectors. Science 1992; 258:123-6.
27. Kim KM, Alber G, Weiser P, Reth M. Differential signaling through the Ig-alpha and Ig-beta components of the B cell antigen receptor. Eur J Immunol 1993; 23:911-6.
28. Sanchez M, Misulovin Z, Burkhardt AL, Mahajan S, Costa T, Franke R, et al. Signal transduction by immunoglobulin is mediated through Igalpha and Igbeta. J Exp Med 1993; 178:1049-55.
29. Demchenko AP. Recognition between flexible protein molecules: induced and assisted folding. J Mol Recognit 2001; 14:42-61.
30. Dyson HJ, Wright PE. Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol 2002; 12:54-60.
31. Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005; 6:197-208.
32. Xu C, Gagnon E, Call ME, Schnell JR, Schwieters CD, Carman CV, et al. Regulation of T cell receptor activation by dynamic membrane binding of the CD3epsilon cytoplasmic tyrosine-based motif. Cell 2008; 135:702-13.
33. Bourhis JM, Receveur-Brechot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, et al. The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. Protein Sci 2005; 14:1975-92.
34. Fletcher CM, McGuire AM, Gingras AC, Li H, Matsuo H, Sonenberg N, et al. 4E binding proteins inhibit the translation factor eIF4E without folded structure. Biochemistry 1998; 37:9-15.
35. Fletcher CM, Wagner G. The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disordered protein. Protein Sci 1998; 7:1639-42.
36. Tomoo K, Matsushita Y, Fujisaki H, Abiko F, Shen X, Taniguchi T, et al. Structural basis for mRNA Cap-Binding regulation of eukaryotic initiation factor 4E by 4E-binding protein, studied by spectroscopic, X-ray crystal structural and molecular dynamics simulation methods. Biochim Biophys Acta 2005; 1753:191-208.
37. Radhakrishnan I, Perez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE. Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell 1997; 91:741-52.
38. Radhakrishnan I, Perez-Alvarado GC, Dyson HJ, Wright PE. Conformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREB. FEBS Lett 1998; 430:317-22.
39. Richards JP, Bachinger HP, Goodman RH, Brennan RG. Analysis of the structural properties of cAMP-responsive element-binding protein (CREB) and phosphorylated CREB. J Biol Chem 1996; 271:13716-23.
40. Hazy E, Tompa P. Limitations of induced folding in molecular recognition by intrinsically disordered proteins. Chemphyschem 2009; 10:1415-9.
41. Dunker AK, Brown CJ, Lawson JD, Iakoucheva LM, Obradovic Z. Intrinsic disorder and protein function. Biochemistry 2002; 41:6573-82.
42. Dunker AK, Brown CJ, Obradovic Z. Identification and functions of usefully disordered proteins. Adv Protein Chem 2002; 62:25-49.
43. Dyson HJ, Wright PE. Equilibrium NMR studies of unfolded and partially folded proteins. Nat Struct Biol 1998; 5:499-503.
44. Dyson HJ, Wright PE. Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance. Adv Protein Chem 2002; 62:311-40.
45. Dyson HJ, Wright PE. Unfolded proteins and protein folding studied by NMR. Chem Rev 2004; 104:3607-22.
46. Eliezer D, Yao J, Dyson HJ, Wright PE. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat Struct Biol 1998; 5:148-55.
47. Zhang O, Forman-Kay JD, Shortle D, Kay LE. Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterization of unfolded, partially folded and folded proteins. J Biomol NMR 1997; 9:181-200.
48. Mittag T, Forman-Kay JD. Atomic-level characterization of disordered protein ensembles. Curr Opin Struct Biol 2007; 17:3-14.
49. Receveur-Brechot V, Bourhis JM, Uversky VN, Canard B, Longhi S. Assessing protein disorder and induced folding. Proteins 2006; 62:24-45.
50. Zuiderweg ER. Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry 2002; 41:1-7.
51. Slupsky CM, Gentile LN, McIntosh LP. Assigning the NMR spectra of aromatic amino acids in proteins: analysis of two Ets pointed domains. Biochem Cell Biol 1998; 76:379-90.
52. Duchardt E, Sigalov AB, Aivazian D, Stern LJ, Schwalbe H. Structure Induction of the T-Cell Receptor zeta-Chain upon Lipid Binding Investigated by NMR Spectroscopy. Chembiochem 2007; 8:820-7.
53. Schaefer TM, Bell I, Fallert BA, Reinhart TA. The T-cell receptor zeta chain contains two homologous domains with which simian immunodeficiency virus Nef interacts and mediates down-modulation. J Virol 2000; 74:3273-83.
54. Sigalov AB. Multichain immune recognition receptor signaling: different players, same game? Trends Immunol 2004; 25:583-9.
55. Wucherpfennig KW, Gagnon E, Call MJ, Huseby ES, Call ME. Structural biology of the T-cell receptor: insights into receptor assembly, ligand recognition and initiation of signaling. Cold Spring Harb Perspect Biol 2010; 2:5140.
56. Sigalov AB. Membrane binding of intrinsically disordered proteins: Critical importance of an appropriate membrane model. Self/Nonself-Immune Recognition and Signaling 2010; 1:129-32.
57. Sigalov AB. Protein intrinsic disorder and oligomericity in cell signaling. Mol Biosyst 2010; 6:451-61.