Characterization and Hsp104-induced artificial clearance of familial ALS-related SOD1 aggregates

Biochemical and Biophysical Research Communications

Volumn 434, Issue 3, 2013, Pages 521-526

  Kim, Yongmin ^a   Park, Ju Hwang ^a   Jang, Ja Young ^a   Rhim, Hyangshuk ^b   Kang, Seongman ^a  

^a Korea University   (South Korea)

^b The Catholic University of Korea   (South Korea)

Author keywords

Amyotrophic lateral sclerosis; FLIP; Hsp104; Mutant SOD1; SOD1 aggregate

Indexed keywords

ADENOSINE TRIPHOSPHATE; COPPER ZINC SUPEROXIDE DISMUTASE; HEAT SHOCK PROTEIN 104; MUTANT PROTEIN; PROTEIN AGGREGATE; HEAT SHOCK PROTEIN; HSP104 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SUPEROXIDE DISMUTASE;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL CELL; ARTICLE; BLEACHING; CELL NUCLEUS MEMBRANE; CONFOCAL MICROSCOPY; CYTOPLASM; FLUORESCENCE RECOVERY AFTER PHOTOBLEACHING; FLUORESCENCE RESONANCE ENERGY TRANSFER; MOUSE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN HYDROLYSIS; YEAST CELL; ANIMAL; ENZYMOLOGY; GENETICS; HUMAN; HYDROLYSIS; METABOLISM; PHYSIOLOGY;

SACCHAROMYCES CEREVISIAE;

ADENOSINE TRIPHOSPHATE; AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEAT-SHOCK PROTEINS; HUMANS; HYDROLYSIS; MICE; MUTANT PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SUPEROXIDE DISMUTASE;

MLCS; MLOWN;

EID: 84880488965     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.03.107     Document Type: Article

References (27)

1. M. Cozzolino, A. Ferri, M.T. Carri, Amyotrophic lateral sclerosis: from current developments in the laboratory to clinical implications, Antioxid. Redox Signal. 10 (2008) 405-443.
2. L.I. Bruijn, T.M. Miller, D.W. Cleveland, Unraveling the mechanisms involved in motor neuron degeneration in ALS, Annu. Rev. Neurosci. 27 (2004) 723-749.
3. D.R. Rosen, T. Siddique, D. Patterson, D.A. Figlewicz, P. Sapp, A. Hentati, D. Donaldson, J. Goto, J.P. O'Regan, H.X. Deng, et al., Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis, Nature 362 (1993) 59-62.
4. B.J. Turner, K. Talbot, Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS, Prog. Neurobiol. 85 (2008) 94-134.
5. T. Fujisawa, K. Homma, N. Yamaguchi, H. Kadowaki, N. Tsuburaya, I. Naguro, A. Matsuzawa, K. Takeda, Y. Takahashi, J. Goto, S. Tsuji, H. Nishitoh, H. Ichijo, A novel monoclonal antibody reveals a conformational alteration shared by amyotrophic lateral sclerosis-linked SOD1 mutants, Ann. Neurol. 72 (2012) 739-749.
6. J.L. Gonzalez de Aguilar, A. Echaniz-Laguna, A. Fergani, F. Rene, V. Meininger, J.P. Loeffler, L. Dupuis, Amyotrophic lateral sclerosis: all roads lead to Rome, J. Neurochem. 101 (2007) 1153-1160.
7. E. Foran, D. Trotti, Glutamate transporters and the excitotoxic path to motor neuron degeneration in amyotrophic lateral sclerosis, Antioxid. Redox Signal. 11 (2009) 1587-1602.
8. S.J. Weisberg, R. Lyakhovetsky, A.C. Werdiger, A.D. Gitler, Y. Soen, D. Kaganovich, Compartmentalization of superoxide dismutase 1 (SOD1G93A) aggregates determines their toxicity, Proc. Natl. Acad. Sci. USA 109 (2012) 15811-15816.
9. H. Witan, A. Kern, I. Koziollek-Drechsler, R. Wade, C. Behl, A.M. Clement, Heterodimer formation of wild-type and amyotrophic lateral sclerosis-causing mutant Cu/Zn-superoxide dismutase induces toxicity independent of protein aggregation, Hum. Mol. Genet. 17 (2008) 1373-1385.
10. J.M. Shefner, A.G. Reaume, D.G. Flood, R.W. Scott, N.W. Kowall, R.J. Ferrante, D.F. Siwek, M. Upton-Rice, R.H. Brown Jr., Mice lacking cytosolic copper/zinc superoxide dismutase display a distinctive motor axonopathy, Neurology 53 (1999) 1239-1246.
11. S. Lee, M.E. Sowa, J.M. Choi, F.T. Tsai, The ClpB/Hsp104 molecular chaperone - a protein disaggregating machine, J. Struct. Biol. 146 (2004) 99-105.
12. M.E. DeSantis, E.H. Leung, E.A. Sweeny, M.E. Jackrel, M. Cushman-Nick, A. Neuhaus-Follini, S. Vashist, M.A. Sochor, M.N. Knight, J. Shorter, Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients, Cell 151 (2012) 778-793.
13. A.B. Biter, J. Lee, N. Sung, F.T. Tsai, S. Lee, Functional analysis of conserved cis- and trans-elements in the Hsp104 protein disaggregating machine, J. Struct. Biol. 179 (2012) 172-180.
14. B. Moosavi, J. Wongwigkarn, M.F. Tuite, Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagation, Yeast 27 (2010) 167-179.
15. C. Vacher, L. Garcia-Oroz, D.C. Rubinsztein, Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington's disease, Hum. Mol. Genet. 14 (2005) 3425-3433.
16. C. Lo Bianco, J. Shorter, E. Regulier, H. Lashuel, T. Iwatsubo, S. Lindquist, P. Aebischer, Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease, J. Clin. Invest. 118 (2008) 3087-3097.
17. J. Shorter, Hsp104: a weapon to combat diverse neurodegenerative disorders, Neurosignals 16 (2008) 63-74.
18. S. Lee, S. Hong, S. Kim, S. Kang, Ataxin-1 occupies the promoter region of E-cadherin in vivo and activates CtBP2-repressed promoter, Biochim. Biophys. Acta 2011 (1813) 713-722.
19. E.J. Yoon, H.J. Park, G.Y. Kim, H.M. Cho, J.H. Choi, H.Y. Park, J.Y. Jang, H.S. Rhim, S.M. Kang, Intracellular amyloid beta interacts with SOD1 and impairs the enzymatic activity of SOD1: implications for the pathogenesis of amyotrophic lateral sclerosis, Exp. Mol. Med. 41 (2009) 611-617.
20. M.A. Rizzo, G.H. Springer, B. Granada, D.W. Piston, An improved cyan fluorescent protein variant useful for FRET, Nat. Biotechnol. 22 (2004) 445-449.
21. T. Nagai, K. Ibata, E.S. Park, M. Kubota, K. Mikoshiba, A. Miyawaki, A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications, Nat. Biotechnol. 20 (2002) 87-90.
22. B. Bosl, V. Grimminger, S. Walter, Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides, J. Biol. Chem. 280 (2005) 38170-38176.
23. Y.J. Shyu, C.D. Suarez, C.D. Hu, Visualization of AP-1 NF-kappaB ternary complexes in living cells by using a BiFC-based FRET, Proc. Natl. Acad. Sci. USA 105 (2008) 151-156.
24. M. Arimon, V. Grimminger, F. Sanz, H.A. Lashuel, Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrils, J. Mol. Biol. 384 (2008) 1157-1173.
25. G. Matsumoto, A. Stojanovic, C.I. Holmberg, S. Kim, R.I. Morimoto, Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates, J. Cell Biol. 171 (2005) 75-85.
26. P.C. Ferreira, F. Ness, S.R. Edwards, B.S. Cox, M.F. Tuite, The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation, Mol. Microbiol. 40 (2001) 1357-1369.
27. J. Weibezahn, C. Schlieker, B. Bukau, A. Mogk, Characterization of a trap mutant of the AAA+ chaperone ClpB, J. Biol. Chem. 278 (2003) 32608-32617.