Six SQSTM1 mutations in a Chinese amyotrophic lateral sclerosis cohort

References

• Hardiman O, van den Berg LH, Kiernan MC. Clinical diagnosis and management of amyotrophic lateral sclerosis. Nat Rev Neurol. 2011;7:639–49.
   PubMed Web of Science ®Google Scholar
• Deng HX, Hentati A, Tainer JA, Iqbal Z, Cayabyab A, Hung WY, et al. Amyotrophic lateral sclerosis and structural defects in Cu/Zn superoxide dismutase. Science. 1993;261: 1047–51.
   PubMed Web of Science ®Google Scholar
• Rosen DR, Siddique T, Patterson D, Figlewicz DA, Sapp P, Hentati A, et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 1993;362:59–62.
   PubMed Web of Science ®Google Scholar
• Dejesus-Hernandez M, Mackenzie IR, Boeve BF, Boxer AL, Baker M , Rutherford NJ, et al. Expanded GGGGCC hexanucleotide repeat in non-coding region of C9orf72 causes chromosome 9p-linked FTD and ALS. Neuron. 2011; 72:245–56.
   PubMed Web of Science ®Google Scholar
• Renton AE, Majounie E, Waite A, Simón-Sánchez J, Rollinson S, Gibbs JR, et al. A hexanucleotide repeat expansion in C9orf72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron. 2011;72:257–68.
   PubMed Web of Science ®Google Scholar
• Majounie E, Renton AE, Mok K, Dopper EG, Waite A, Rollinson S, et al. Frequency of the C9orf72 hexanucleotide repeat expansion in patients with amyotrophic lateral sclerosis and frontotemporal dementia: a cross-sectional study. Lancet Neurol. 2012;11:323–30.
   PubMed Web of Science ®Google Scholar
• Liu R, Tang L, Cai B, Liu XL, Ye S, Ma Y, et al. C9orf72 repeat expansion are not detected in Chinese patients with familial ALS. Amyotroph Lateral Scler Frontotemporal Degener. 2013;14:630–1.
   PubMed Web of Science ®Google Scholar
• Zou ZY , Li XG , Liu MS , Cui LY. Screening for C9orf72 repeat expansions in Chinese amyotrophic lateral sclerosis patients. Neurobiol Aging. 2013;34:1710.e5–6.
   PubMed Web of Science ®Google Scholar
• Ogaki K, Li Y, Atsuta N, Tomiyama H, Funayama M, Watanabe H, et al. Analysis of C9orf72 repeat expansion in 563 Japanese patients with amyotrophic lateral sclerosis. Neurobiol Aging. 2012;33:2527.e11–6.
   PubMed Web of Science ®Google Scholar
• Jang JH, Kwon MJ, Choi WJ, Oh KW, Koh SH, Ki CS, et al. Analysis of the C9orf72 hexanucleotide repeat expansion in Korean patients with familial and sporadic amyotrophic lateral sclerosis. Neurobiol Aging. 2013;34:1311.e7–9.
   PubMed Web of Science ®Google Scholar
• Kabashi E, Valdmanis PN, Dion P, Spiegelman D, McConkey BJ , Vandevelde C, et al. TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat Genet. 2008;40:572–4.
   PubMed Web of Science ®Google Scholar
• Sreedharan J, Blair IP, Tripathi VB, Hu X, Vance C, Rogelj B, et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science. 2008;319:1668–72.
   PubMed Web of Science ®Google Scholar
• Kwiatkowski TJ Jr, Bosco DA, Leclerc AL, Tamrazian E, Vanderburg CR, Russ C, et al. Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science. 2009;323:1205–8.
   PubMed Web of Science ®Google Scholar
• Vance C, Rogelj B, Hortobagyi T, de Vos KJ, Nishimura AL, Sreedharan J, et al. Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science. 2009;323:1208–11.
   PubMed Web of Science ®Google Scholar
• Deng HX, Chen W, Hong ST , Boycott KM , Gorrie GH, Siddique N, et al. Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia. Nature. 2011;477:211–5.
   PubMed Web of Science ®Google Scholar
• Maruyama H, Morino H, Ito H, Izumi Y, Kato H, Watanabe Y, et al. Mutations of optineurin in amyotrophic lateral sclerosis. Nature. 2010;465:223–6.
   PubMed Web of Science ®Google Scholar
• Sleegers K, Brouwers N, Maurer-Stroh S, van Es MA, van Damme P, van Vught PW, et al. Progranulin genetic variability contributes to amyotrophic lateral sclerosis. Neurology. 2008;71:253–9.
   PubMed Web of Science ®Google Scholar
• Wu CH, Fallini C, Ticozzi N, Keagle PJ, Sapp PC, Piotrowska K, et al. Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis. Nature. 2012;488: 499–503.
   PubMed Web of Science ®Google Scholar
• Johnson JO, Mandrioli J, Benatar M, Abramzon Y, van Deerlin VM, Trojanowski JQ, et al. Exome sequencing reveals VCP mutations as a cause of familial ALS. Neuron. 2010;68:857–64.
   PubMed Web of Science ®Google Scholar
• Droppelmann CA, Wang J, Campos-Melo D, Keller B, Volkening K, Hegele RA, et al. Detection of a novel frameshift mutation and regions with homozygosis within ARHGEF28 gene in familial amyotrophic lateral sclerosis. Amyotroph Lateral Scler Frontotemporal Degener. 2013;14:444–51.
   PubMed Web of Science ®Google Scholar
• Shaw BF, Lelie HL, Durazo A , Nersissian AM , Xu G, Chan PK, et al. Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1. J Biol Chem. 2008;283:8340–50.
   PubMed Web of Science ®Google Scholar
• Stieber A, Gonatas JO, Gonatas NK. Aggregates of mutant protein appear progressively in dendrites, in periaxonal processes of oligodendrocytes, and in neuronal and astrocytic perikarya of mice expressing the SOD1-G93A mutation of familial amyotrophic lateral sclerosis. J Neurol Sci. 2000; 177:114–23.
   PubMed Web of Science ®Google Scholar
• Arai T, Hasegawa M , Akiyama H , Ikeda K , Nonaka T, Mori H, et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun. 2006;351:602–11.
   PubMed Web of Science ®Google Scholar
• Neumann M, Sampathu DM , Kwong LK, Truax AC, Micsenyi MC, Chou TT, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science. 2006;314:130–3.
   PubMed Web of Science ®Google Scholar
• Mizuno Y, Amari M, Takatama M, Aizawa H, Mihara B, Okamoto K. Immunoreactivities of p62, an ubiqutin-binding protein, in the spinal anterior horn cells of patients with amyotrophic lateral sclerosis. J Neurol Sci. 2006;249:13–8.
   PubMed Web of Science ®Google Scholar
• Zatloukal K, Stumptner C, Fuchsbichler A, Heid H, Schnoelzer M, Kenner L, et al. p62 is a common component of cytoplasmic inclusions in protein aggregation diseases. Am J Pathol. 2002;160:255–63.
   PubMed Web of Science ®Google Scholar
• Gal J, Ström AL, Kilty R, Zhang F, Zhu H. p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis. J Biol Chem. 2007; 282:11068–77.
   PubMed Web of Science ®Google Scholar
• Ramesh Babu J, Lamar Seibenhener M, Peng J, Strom AL, Kemppainen R, Cox N, et al. Genetic inactivation of p62 leads to accumulation of hyperphosphorylated tau and neurodegeneration. J Neurochem. 2008;106:107–20.
   PubMed Web of Science ®Google Scholar
• Moscat J, Diaz-Meco MT, Wooten MW. Signal integration and diversification through the p62 scaffold protein. Trends Biochem Sci. 2007;32:95–100.
   PubMed Web of Science ®Google Scholar
• Lin X, Li S, Zhao Y, Ma X, Zhang K, He X, et al. Interaction domains of p62: a bridge between p62 and selective autophagy. DNA. Cell Biol. 2013;32:220–7.
   PubMed Web of Science ®Google Scholar
• Fecto F, Yan J, Vemula SP, Liu E, Yang Y, Chen W, et al. SQSTM1 mutations in familial and sporadic amyotrophic lateral sclerosis. Arch Neurol. 2011;68:1440–6.
   PubMed Web of Science ®Google Scholar
• Hirano M, Nakamura Y, Saigoh K, Sakamoto H, Ueno S, Isono C, et al. Mutations in the gene encoding p62 in Japanese patients with amyotrophic lateral sclerosis. Neurology. 2013;80:458–63.
   PubMed Web of Science ®Google Scholar
• Rubino E, Rainero I, Chiò A, Rogaeva E, Galimberti D, Fenoglio P, et al. SQSTM1 mutations in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Neurology. 2012;79:1556–62.
   PubMed Web of Science ®Google Scholar
• Teyssou E, Takeda T, Lebon V, Boillée S, Doukouré B, Bataillon G, et al. Mutations in SQSTM1 encoding p62 in amyotrophic lateral sclerosis: genetics and neuropathology. Acta Neuropathol. 2013;125:511–22.
   PubMed Web of Science ®Google Scholar
• Chen Y, Zheng ZZ, Chen X, Huang R, Yang Y, Yuan L, et al. SQSTM1 mutations in Han Chinese populations with sporadic amyotrophic lateral sclerosis. Neurobiol Aging. 2014;35:726.e7–9.
   PubMed Web of Science ®Google Scholar
• Kwok CT, Morris A, de Belleroche JS. Sequestosome-1 (SQSTM1) sequence variants in ALS cases in the UK: prevalence and coexistence of SQSTM1 mutations in ALS kindred with PDB. Eur J Hum Genet. 2014;22:492–6.
   PubMed Web of Science ®Google Scholar
• Le Ber I, Camuzat A, Guerreiro R, Bouya-Ahmed K, Bras J, Nicolas G, et al. SQSTM1 mutations in French patients with frontotemporal dementia or frontotemporal dementia with amyotrophic lateral sclerosis. JAMA Neurol. 2013;70: 1403–10.
   PubMed Web of Science ®Google Scholar
• Shimizu H, Toyoshima Y, Shiga A, Yokoseki A, Arakawa K, Sekine Y, et al. Sporadic ALS with compound heterozygous mutations in the SQSTM1 gene. Acta Neuropathol. 2013;126:453–9.
   PubMed Web of Science ®Google Scholar
• Czaplinski A, Yen AA, Simpson EP, Appel SH. Predictability of disease progression in amyotrophic lateral sclerosis. Muscle Nerve. 2006;34:702–8.
   PubMed Web of Science ®Google Scholar
• Louwerse ES, Visser CE, Bossuyt PM, Weverling GJ. Amyotrophic lateral sclerosis: mortality risk during the course of the disease and prognostic factors. The Netherlands ALS Consortium. J Neurol Sci. 1997;152 (Suppl 1):S10–7.
   Google Scholar
• Kaufmann P, Levy G, Thompson JL, Delbene ML, Battista V, Gordon PH, et al. The ALSFRS-R predicts survival time in an ALS clinic population. Neurology. 2005;64:38–43.
   PubMed Web of Science ®Google Scholar
• Kimura F, Fujimura C, Ishida S, Nakajima H, Furutama D, Uehara H, et al. Progression rate of ALSFRS-R at time of diagnosis predicts survival time in ALS. Neurology. 2006; 66:265–7.
   PubMed Web of Science ®Google Scholar
• Kollewe K, Mauss U, Krampfl K, Petri S, Dengler R, Mohammadi B. ALSFRS-R score and its ratio: a useful predictor for ALS progression. J Neurol Sci. 2008;275:69–73.
   PubMed Web of Science ®Google Scholar
• Brooks BR, Miller RG, Swash M, Munsat TL, World Federation of Neurology Research Group on Motor Neuron Diseases. EI Escorial revisited: revised criteria for the diagnosis of amyotrophic lateral sclerosis. Amyotroph Lateral Scler Other Motor Neuron Disord. 2000;1:293–9.
   PubMed Web of Science ®Google Scholar
• Byrne S, Bede P, Elamin M, Kenna K, Lynch C, McLaughlin R, et al. Proposed criteria for familial amyotrophic lateral sclerosis. Amyotroph Lateral Scler. 2011;12:157–9.
   PubMed Web of Science ®Google Scholar
• Du Y, Wooten MC, Wooten MW. Oxidative damage to the promoter region of SQSTM1/p62 is common to neurodegenerative disease. Neurobiol Dis. 2009;35:302–10.
   PubMed Web of Science ®Google Scholar
• Bodmer W, Bonilla C. Common and rare variants in multifactorial susceptibility to common diseases. Nat Genet. 2008;40:695–701.
   PubMed Web of Science ®Google Scholar
• Rea SL, Walsh JP, Layfield R, Ratajczak T, Xu J. New insights into the role of sequestosome1/p62 mutant proteins in the pathogenesis of Paget’s disease of bone. Endocr Rev. 2013; 34:501–24.
   PubMed Web of Science ®Google Scholar
• Lamark T, Perander M, Outzen H, Kristiansen K, Øvervatn A, Michaelsen E, et al. Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins. J Biol Chem. 2003;278:34568–81.
   PubMed Web of Science ®Google Scholar
• Jadhav TS, Wooten MW, Wooten MC. Mining the TRAF6/p62 interactome for a selective ubiquitination motif. BMC Proc 2011;5(Suppl 2):S4.
   PubMedGoogle Scholar
• Johansen T, Lamark T. Selective autophagy mediated by autophagic adapter proteins. Autophagy. 2011;7:279–96.
   PubMed Web of Science ®Google Scholar
• Pursiheimo JP, Rantanen K, Heikkinen PT, Johansen T, Jaakkola PM. Hypoxia-activated autophagy accelerates degradation of SQSTM1/P62. Oncogene. 2009;28:334–44.
   PubMed Web of Science ®Google Scholar
• Cavey JR, Ralston SH, Sheppard PW, Ciani B, Gallagher TR, Long JE, et al. Loss of ubiquitin binding is a unifying mechanism by which mutations of SQSTM1 cause Paget's disease of bone. Calcif Tissue Int. 2006;78:271–7.
   PubMed Web of Science ®Google Scholar
• Wooten MW, Geetha T, Seibenhener ML, Babu JR, Diaz-Meco MT, Moscat J. The p62 scaffold regulates nerve growth factor-induced NF-kappaB activation by influencing TRAF6 polyubiquitination. J Biol Chem. 2005;280:35625–9.
   PubMed Web of Science ®Google Scholar