Role of High Mobility Group Box 1 (HMGB1) in SCA17 pathogenesis

PLoS ONE

Volumn 9, Issue 12, 2014, Pages

  Lee, Li Ching ^a   Chen, Chiung Mei ^b   Wang, Pin Rong ^a   Su, Ming Tsan ^a   Lee Chen, Guey Jen ^a   Chang, Chun Yen ^a  

^a NATIONAL TAIWAN NORMAL UNIVERSITY   (Taiwan)

^b CHANG GUNG UNIVERSITY COLLEGE OF MEDICINE   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

HIGH MOBILITY GROUP B1 PROTEIN; REACTIVE OXYGEN METABOLITE; TATA BINDING PROTEIN; HEAT SHOCK PROTEIN; MOLECULAR CHAPERONE GRP78;

ARTICLE; AUTOPHAGY; CELL NUCLEUS; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOPLASM; GENE; GENE EXPRESSION; HEK293 CELL LINE; HSPA5 GENE; HUMAN; HUMAN CELL; NERVE CELL; NERVE FIBER GROWTH; OXIDATIVE STRESS; PATHOGENESIS; PROTEIN AGGREGATION; SPINOCEREBELLAR ATAXIA TYPE 17; SPINOCEREBELLAR DEGENERATION; TRANSCRIPTION REGULATION; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; PHYSIOLOGY;

AUTOPHAGY; CYTOPLASM; GENE EXPRESSION REGULATION; HEAT-SHOCK PROTEINS; HEK293 CELLS; HMGB1 PROTEIN; HUMANS; OXIDATIVE STRESS; SPINOCEREBELLAR ATAXIAS; TATA-BOX BINDING PROTEIN;

EID: 84920198107     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0115809     Document Type: Article

References (37)

1. Burley SK, Roeder RG (1996) Biochemistry and structural biology of transcription factor IID (TFIID). Annu Rev Biochem 65: 769-799.
2. Horikoshi M, Yamamoto T, Ohkuma Y, Weil PA, Roeder RG (1990) Analysis of structure-function relationships of yeast TATA box binding factor TFIID. Cell 61: 1171-1178.
3. Lescure A, Lutz Y, Eberhard D, Jacq X, Krol A, et al. (1994) The N-terminal domain of the human TATA-binding protein plays a role in transcription from TATA-containing RNA polymerase II and III promoters. EMBO J 13: 1166-1175.
4. Gostout B, Liu Q, Sommer SS (1993) "Cryptic" repeating triplets of purines and pyrimidines (cRRY(i)) are frequent and polymorphic: analysis of coding cRRY(i) in the proopiomelanocortin (POMC) and TATA-binding protein (TBP) genes. Am J Hum Genet 52: 1182-1190.
5. Silveira I, Miranda C, Guimaraes L, Moreira MC, Alonso I, et al. (2002) Trinucleotide repeats in 202 families with ataxia: a small expanded (CAG)n allele at the SCA17 locus. Arch Neurol 59: 623-629.
6. Maltecca F, Filla A, Castaldo I, Coppola G, Fragassi NA, et al. (2003) Intergenerational instability and marked anticipation in SCA-17. Neurology 61: 1441-1443.
7. Koide R, Kobayashi S, Shimohata T, Ikeuchi T, Maruyama M, et al. (1999) A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: a new polyglutamine disease? Hum Mol Genet 8: 2047-2053.
8. Nakamura K, Jeong SY, Uchihara T, Anno M, Nagashima K, et al. (2001) SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein. Hum Mol Genet 10: 1441-1448.
9. Ge H, Roeder RG (1994) The high mobility group protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein. J Biol Chem 269: 17136-17140.
10. Zappavigna V, Falciola L, Helmer-Citterich M, Mavilio F, Bianchi ME (1996) HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activation. EMBO J 15: 4981-4991.
11. Landsman D, Bustin M (1993) A signature for the HMG-1 box DNA-binding proteins. Bioessays 15: 539-546.
12. Sutrias-Grau M, Bianchi ME, Bernues J (1999) High mobility group protein 1 interacts specifically with the core domain of human TATA box-binding protein and interferes with transcription factor IIB within the pre-initiation complex. J Biol Chem 274: 1628-1634.
13. Das D, Scovell WM (2001) The binding interaction of HMG-1 with the TATA-binding protein/TATA complex. J Biol Chem 276: 32597-32605.
14. Scaffidi P, Misteli T, Bianchi ME (2002) Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature 418: 191-195.
15. Park JS, Svetkauskaite D, He Q, Kim JY, Strassheim D, et al. (2004) Involvement of toll-like receptors 2 and 4 in cellular activation by high mobility group box 1 protein. J Biol Chem 279: 7370-7377.
16. Tang D, Kang R, Livesey KM, Cheh CW, Farkas A, et al. (2010) Endogenous HMGB1 regulates autophagy. J Cell Biol 190: 881-892.
17. Tang D, Kang R, Livesey KM, Zeh HJ 3rd, Lotze MT (2011) High mobility group box 1 (HMGB1) activates an autophagic response to oxidative stress. Antioxid Redox Signal 15: 2185-2195.
18. Min HJ, Ko EA, Wu J, Kim ES, Kwon MK, et al. (2013) Chaperone-like activity of high-mobility group box 1 protein and its role in reducing the formation of polyglutamine aggregates. J Immunol 190: 1797-1806.
19. Jimenez-Sanchez M, Thomson F, Zavodszky E, Rubinsztein DC (2012) Autophagy and polyglutamine diseases. Prog Neurobiol 97: 67-82.
20. Qi ML, Tagawa K, Enokido Y, Yoshimura N, Wada Y, et al. (2007) Proteome analysis of soluble nuclear proteins reveals that HMGB1/2 suppress genotoxic stress in polyglutamine diseases. Nat Cell Biol 9: 402-414.
21. Lee LC, Chen CM, Chen FL, Lin PY, Hsiao YC, et al. (2009) Altered expression of HSPA5, HSPA8 and PARK7 in spinocerebellar ataxia type 17 identified by 2-dimensional fluorescence difference in gel electrophoresis. Clin Chim Acta 400: 56-62.
22. Chen CM, Lee LC, Soong BW, Fung HC, Hsu WC, et al. (2010) SCA17 repeat expansion: mildly expanded CAG/CAA repeat alleles in neurological disorders and the functional implications. Clin Chim Acta 411: 375-380.
23. Wyttenbach A, Sauvageot O, Carmichael J, Diaz-Latoud C, Arrigo AP, et al. (2002) Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum Mol Genet 11: 1137-1151.
24. Scherz-Shouval R, Shvets E, Fass E, Shorer H, Gil L, et al. (2007) Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J 26: 1749-1760.
25. Tanida I, Ueno T, Kominami E (2004) LC3 conjugation system in mammalian autophagy. Int J Biochem Cell Biol 36: 2503-2518.
26. Shimohata T, Onodera O, Tsuji S (2000) Interaction of expanded polyglutamine stretches with nuclear transcription factors leads to aberrant transcriptional regulation in polyglutamine diseases. Neuropathology 20: 326-333.
27. Friedman MJ, Shah AG, Fang ZH, Ward EG, Warren ST, et al. (2007) Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration. Nat Neurosci 10: 1519-1528.
28. Huang S, Ling JJ, Yang S, Li XJ, Li S (2011) Neuronal expression of TATA box-binding protein containing expanded polyglutamine in knock-in mice reduces chaperone protein response by impairing the function of nuclear factor-Y transcription factor. Brain 134: 1943-1958.
29. Lee LC, Chen CM, Wang HC, Hsieh HH, Chiu IS, et al. (2012) Role of the CCAAT-binding protein NFY in SCA17 pathogenesis. PLoS One 7: e35302.
30. Wang M, Ye R, Barron E, Baumeister P, Mao C, et al. (2010) Essential role of the unfolded protein response regulator GRP78/BiP in protection from neuronal apoptosis. Cell Death Differ 17: 488-498.
31. Maity SN, de Crombrugghe B (1998) Role of the CCAAT-binding protein CBF/NF-Y in transcription. Trends Biochem Sci 23: 174-178.
32. Mantovani R (1999) The molecular biology of the CCAAT-binding factor NF-Y. Gene 239: 15-27.
33. Stros M, Polanska E, Struncova S, Pospisilova S (2009) HMGB1 and HMGB2 proteins up-regulate cellular expression of human topoisomerase IIalpha. Nucleic Acids Res 37: 2070-2086.
34. Mizushima N, Levine B, Cuervo AM, Klionsky DJ (2008) Autophagy fights disease through cellular self-digestion. Nature 451: 1069-1075.
35. Levine B, Kroemer G (2008) Autophagy in the pathogenesis of disease. Cell 132: 27-42.
36. Menzies FM, Huebener J, Renna M, Bonin M, Riess O, et al. (2010) Autophagy induction reduces mutant ataxin-3 levels and toxicity in a mouse model of spinocerebellar ataxia type 3. Brain 133: 93-104.
37. Takahashi T, Katada S, Onodera O (2010) Polyglutamine diseases: where does toxicity come from? what is toxicity? where are we going? J Mol Cell Biol 2: 180-191.