HspB2/myotonic dystrophy protein kinase binding protein (MKBP) as a novel molecular chaperone: Structural and functional aspects

PLoS ONE

Volumn 7, Issue 1, 2012, Pages

  Prabhu, Sankaralingam ^a   Raman, Bakthisaran ^a   Ramakrishna, Tangirala ^a   Rao, Ch Mohan ^a  

^a CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ALCOHOL DEHYDROGENASE; ALPHA CRYSTALLIN; ALPHA SYNUCLEIN; AMYLOID; CHAPERONE; CITRATE SYNTHASE; DITHIOTHREITOL; INSULIN; MYOTONIC DYSTROPHY PROTEIN KINASE BINDING PROTEIN; PROTEIN HSPB2; RECOMBINANT PROTEIN; SMALL HEAT SHOCK PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG; CRYSTALLIN; HEAT SHOCK PROTEIN 27; HSPB2 PROTEIN, HUMAN;

ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ESCHERICHIA COLI; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENCE SPECTROSCOPY; HEAT; HYDROPHOBICITY; MOLECULAR CLONING; OLIGOMERIZATION; PRECIPITATION; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN TARGETING; SEDIMENTATION RATE; ULTRAVIOLET RADIATION; CELL CULTURE; CHEMICAL PHENOMENA; CHEMISTRY; GENETICS; HUMAN; METABOLISM; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN SUBUNIT; SPECTROFLUOROMETRY;

ALPHA-SYNUCLEIN; AMYLOID; CELLS, CULTURED; CIRCULAR DICHROISM; CRYSTALLINS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; FLUORESCENCE RESONANCE ENERGY TRANSFER; HSP27 HEAT-SHOCK PROTEINS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MOLECULAR CHAPERONES; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE;

EID: 84855838615     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0029810     Document Type: Article

References (53)

1. Suzuki A, Sugiyama Y, Hayashi Y, Nyu-i N, Yoshida M, et al. (1998) MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase. J Cell Biol 140: 1113-1124.1.
2. Brook JD, McCurrach ME, Harley HG, Buckler AJ, Church D, et al. (1992) Molecular basis of myotonic dystrophy: expansion of a trinucleotide (CTG) repeat at the 3′ end of a transcript encoding a protein kinase family member. Cell 68: 799-808.
3. Fu YH, Pizzuti A, Fenwick RG, King J, Rajnarayan S, et al. (1992) An unstable triplet repeat in a gene related to myotonic muscular dystrophy. Science 255: 1256-1258.
4. Mahadevan M, Tsilfidis C, Sabourin L, Shutler G, Amemiya C, et al. (1992) Myotonic dystrophy mutation: an unstable CTG repeat in the 3′ untranslated region of the gene. Science 255: 1253-1255.
5. Iwaki A, Nagano T, Nakagawa M, Iwaki T, Fukumaki Y, (1997) Identification and characterization of the gene encoding a new member of the alpha-crystallin/small hsp family, closely linked to the alphaB-crystallin gene in a head-to-head manner. Genomics 45: 386-394.
6. Suzuki A, Sugiyama Y, Hayashi Y, Nyu-i N, Yoshida M, et al. (1998) MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase. J Cell Biol 140: 1113-1124.
7. Golenhofen N, Perng M, Quinlan R, Drenckhahn D, (2004) Comparison of the small heat shock proteins alphaB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle. Histochem Cell Biol 122: 415-425.
8. Verschuure P, Tatard C, Boelens W, Grongnet J, David J, (2003) Expression of small heat shock proteins HspB2, HspB8, Hsp20 and cvHsp in different tissues of the perinatal developing pig. Eur J Cell Biol 82: 523-530.
9. Shama K, Suzuki A, Harada K, Fujitani N, Kimura H, et al. (1999) Transient up-regulation of myotonic dystrophy protein kinase-binding protein, MKBP, and HSP27 in the neonatal myocardium. Cell Struct Funct 24: 1-4.
10. Yoshida K, Aki T, Harada K, Shama K, Kamoda Y, et al. (1999) Translocation of HSP27 and MKBP in ischemic heart. Cell Struct Funct 24: 181-185.
11. Pinz I, Robbins J, Rajasekaran N, Benjamin I, Ingwall J, (2008) Unmasking different mechanical and energetic roles for the small heat shock proteins CryAB and HSPB2 using genetically modified mouse hearts. FASEB J 22: 84-92.
12. Nakagawa M, Tsujimoto N, Nakagawa H, Iwaki T, Fukumaki Y, et al. (2001) Association of HSPB2, a member of the small heat shock protein family, with mitochondria. Exp Cell Res 271: 161-168.
13. Sugiyama Y, Suzuki A, Kishikawa M, Akutsu R, Hirose T, et al. (2000) Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation. J Biol Chem 275: 1095-1104.
14. Wilhelmus M, Otte-Höller I, Wesseling P, de Waal R, Boelens W, et al. (2006) Specific association of small heat shock proteins with the pathological hallmarks of Alzheimer's disease brains. Neuropathol Appl Neurobiol 32: 119-130.
15. Lehrer S, (1971) Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10: 3254-3263.
16. Schuck P, (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys J 78: 1606-1619.
17. Bova MP, Ding LL, Horwitz J, Fung BK, (1997) Subunit exchange of alphaA-crystallin. J Biol Chem 272: 29511-29517.
18. Bova M, McHaourab H, Han Y, Fung B, (2000) Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations. J Biol Chem 275: 1035-1042.
19. Musci G, Metz G, Tsunematsu H, Berliner L, (1985) 4, 4′-Bis [8-(phenylamino) naphthalene-1-sulfonate] binding to human thrombins: a sensitive exo site fluorescent affinity probe. Biochemistry 24: 2034-2039.
20. Raman B, Rao CM, (1994) Chaperone-like activity and quaternary structure of alpha-crystallin. J Biol Chem 269: 27264-27268.
21. Raman B, Ramakrishna T, Rao CM, (1995) Temperature dependent chaperone-like activity of alpha-crystallin. FEBS Lett 365: 133-136.
22. Das KP, Surewicz WK, (1995) Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett 369: 321-325.
23. Engelhard M, Evans P, (1995) Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates. Protein Sci 4: 1553-1562.
24. Sanger F, (1949) Fractionation of oxidized insulin. Biochem J 44: 126-128.
25. Rogalla T, Ehrnsperger M, Preville X, Kotlyarov A, Lutsch G, et al. (1999) Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. J Biol Chem 274: 18947-18956.
26. Chowdary T, Raman B, Ramakrishna T, Rao C, (2004) Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity. Biochem J 381: 379-387.
27. Kim M, Seit-Nebi A, Marston S, Gusev N, (2004) Some properties of human small heat shock protein Hsp22 (H11 or HspB8). Biochem Biophys Res Commun 315: 796-801.
28. Horwitz J, (1992) Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci U S A 89: 10449-10453.
29. Sun T, Das B, Liang J, (1997) Conformational and functional differences between recombinant human lens alphaA- and alphaB-crystallin. J Biol Chem 272: 6220-6225.
30. Datta S, Rao C, (1999) Differential temperature-dependent chaperone-like activity of alphaA- and alphaB-crystallin homoaggregates. J Biol Chem 274: 34773-34778.
31. Martí M, Tolosa E, Campdelacreu J, (2003) Clinical overview of the synucleinopathies. Mov Disord 18 (Suppl 6): S21-27.
32. Galvin J, Lee V, Trojanowski J, (2001) Synucleinopathies: clinical and pathological implications. Arch Neurol 58: 186-190.
33. Necula M, Chirita C, Kuret J, (2003) Rapid anionic micelle-mediated alpha-synuclein fibrillization in vitro. J Biol Chem 278: 46674-46680.
34. Ahmad M, Ramakrishna T, Raman B, Rao C, (2006) Fibrillogenic and non-fibrillogenic ensembles of SDS-bound human alpha-synuclein. J Mol Biol 364: 1061-1072.
35. Kuwajima K, (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6: 87-103.
36. Ptitsyn OB, (1995) Molten globule and protein folding. Adv Protein Chem 47: 83-229.
37. Kaliman P, Llagostera E, (2008) Myotonic dystrophy protein kinase (DMPK) and its role in the pathogenesis of myotonic dystrophy 1. Cell Signal 20: 1935-1941.
38. Pinz I, Robbins J, Rajasekaran N, Benjamin I, Ingwall J, (2008) Unmasking different mechanical and energetic roles for the small heat shock proteins CryAB and HSPB2 using genetically modified mouse hearts. FASEB J 22: 84-92.
39. van den IJssel P, Norman D, Quinlan R, (1999) Molecular chaperones: small heat shock proteins in the limelight. Curr Biol 9: R103-105.
40. Narberhaus F, (2002) Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol Mol Biol Rev 66: 64-93.
41. Datta S, Rao C, (2000) Packing-induced conformational and functional changes in the subunits of alpha-crystallin. J Biol Chem 275: 41004-41010.
42. Bova M, Huang Q, Ding L, Horwitz J, (2002) Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii. J Biol Chem 277: 38468-38475.
43. Gu L, Abulimiti A, Li W, Chang Z, (2002) Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity. J Mol Biol 319: 517-526.
44. Mandal PK, Pettegrew JW, Masliah E, Hamilton RL, Mandal R, (2006) Interaction between Abeta peptide and alpha synuclein: molecular mechanisms in overlapping pathology of Alzheimer's and Parkinson's in dementia with Lewy body disease. Neurochem Res 31: 1153-1162.
45. Han H, Weinreb PH, Lansbury PT, (1995) The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: is NAC a common trigger or target in neurodegenerative disease? Chem Biol 2: 163-169.
46. Gerthoffer W, Gunst S, (2001) Invited review: focal adhesion and small heat shock proteins in the regulation of actin remodeling and contractility in smooth muscle. J Appl Physiol 91: 963-972.
47. Arrigo A, (2000) sHsp as novel regulators of programmed cell death and tumorigenicity. Pathol Biol (Paris) 48: 280-288.
48. Arrigo A, (1998) Small stress proteins: chaperones that act as regulators of intracellular redox state and programmed cell death. Biol Chem 379: 19-26.
49. Benndorf R, Welsh M, (2004) Shocking degeneration. Nat Genet 36: 547-548.
50. Ciocca D, Calderwood S, (2005) Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 10: 86-103.
51. Sun Y, MacRae T, (2005) The small heat shock proteins and their role in human disease. FEBS J 272: 2613-2627.
52. Danan I, Rashed E, Depre C, (2007) Therapeutic potential of H11 kinase for the ischemic heart. Cardiovasc Drug Rev 25: 14-29.
53. Arrigo A, Simon S, Gibert B, Kretz-Remy C, Nivon M, et al. (2007) Hsp27 (HspB1) and alphaB-crystallin (HspB5) as therapeutic targets. FEBS Lett 581: 3665-3674.