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Volumn 27, Issue 4, 2017, Pages 363-369

The role of p62/SQSTM1 in sporadic inclusion body myositis

Author keywords

LC3; Lys63 linked ubiquitin; p62 SQSTM1; Selective autophagy; Sporadic inclusion body myositis (s IBM)

Indexed keywords

LIGHT CHAIN 3 PROTEIN; MEMBRANE PROTEIN; SEQUESTOSOME 1; UBIQUITIN; UNCLASSIFIED DRUG; P62 PROTEIN, HUMAN; RNA BINDING PROTEIN; SQSTM1 PROTEIN, HUMAN;

EID: 85011012866     PISSN: 09608966     EISSN: 18732364     Source Type: Journal    
DOI: 10.1016/j.nmd.2016.12.009     Document Type: Article
Times cited : (17)

References (39)
  • 1
    • 84920717770 scopus 로고    scopus 로고
    • Inclusion body myositis: a review of clinical and genetic aspects, diagnostic criteria and therapeutic approaches
    • [1] Mastaglia, F.L., Needham, M., Inclusion body myositis: a review of clinical and genetic aspects, diagnostic criteria and therapeutic approaches. J Clin Neurosci 22 (2015), 6–13.
    • (2015) J Clin Neurosci , vol.22 , pp. 6-13
    • Mastaglia, F.L.1    Needham, M.2
  • 3
    • 0347093694 scopus 로고    scopus 로고
    • Expression of lysosome-related proteins and genes in the skeletal muscles of inclusion body myositis
    • [3] Kumamoto, T., Ueyama, H., Tsumura, H., et al. Expression of lysosome-related proteins and genes in the skeletal muscles of inclusion body myositis. Acta Neuropathol 107 (2004), 59–65.
    • (2004) Acta Neuropathol , vol.107 , pp. 59-65
    • Kumamoto, T.1    Ueyama, H.2    Tsumura, H.3
  • 4
    • 34250904159 scopus 로고    scopus 로고
    • Macroautophagy as a pathomechanism in sporadic inclusion body myositis
    • [4] Lünemann, J.D., Schmidt, J., Dalakas, M.C., et al. Macroautophagy as a pathomechanism in sporadic inclusion body myositis. Autophagy 3 (2007), 384–386.
    • (2007) Autophagy , vol.3 , pp. 384-386
    • Lünemann, J.D.1    Schmidt, J.2    Dalakas, M.C.3
  • 5
    • 82355175806 scopus 로고    scopus 로고
    • Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis
    • [5] D'Agostino, C., Nogalska, A., Cacciottolo, M., et al. Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis. Acta Neuropathol 122 (2011), 627–636.
    • (2011) Acta Neuropathol , vol.122 , pp. 627-636
    • D'Agostino, C.1    Nogalska, A.2    Cacciottolo, M.3
  • 6
    • 84886790407 scopus 로고    scopus 로고
    • Overexpression of autophagic proteins in the skeletal muscle of sporadic inclusion body myositis
    • [6] Girolamo, F., Lia, A., Amati, A., et al. Overexpression of autophagic proteins in the skeletal muscle of sporadic inclusion body myositis. Neuropathol Appl Neurobiol 39 (2013), 736–749.
    • (2013) Neuropathol Appl Neurobiol , vol.39 , pp. 736-749
    • Girolamo, F.1    Lia, A.2    Amati, A.3
  • 7
    • 80054025654 scopus 로고    scopus 로고
    • The role of Atg proteins in autophagosome formation
    • [7] Mizushima, N., Yoshimori, T., Ohsumi, Y., The role of Atg proteins in autophagosome formation. Annu Rev Cell Dev Biol 27 (2011), 107–132.
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 107-132
    • Mizushima, N.1    Yoshimori, T.2    Ohsumi, Y.3
  • 9
    • 85005769239 scopus 로고    scopus 로고
    • Comparative utility of LC3, p62 and TDP-43 immunohistochemistry in differentiation of inclusion body myositis from polymyositis and related inflammatory myopathies
    • [9] Hiniker, A., Daniels, B.H., Lee, H.S., et al. Comparative utility of LC3, p62 and TDP-43 immunohistochemistry in differentiation of inclusion body myositis from polymyositis and related inflammatory myopathies. Acta Neuropathol Commun, 1, 2013, 29.
    • (2013) Acta Neuropathol Commun , vol.1 , pp. 29
    • Hiniker, A.1    Daniels, B.H.2    Lee, H.S.3
  • 10
    • 68349097450 scopus 로고    scopus 로고
    • p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis
    • [10] Nogalska, A., Terracciano, C., D'Agostino, C., et al. p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis. Acta Neuropathol 118 (2009), 407–413.
    • (2009) Acta Neuropathol , vol.118 , pp. 407-413
    • Nogalska, A.1    Terracciano, C.2    D'Agostino, C.3
  • 11
    • 81455128284 scopus 로고    scopus 로고
    • Diagnostic value of markers of muscle degeneration in sporadic inclusion body myositis
    • [11] Dubourg, O., Wanschitz, J., Maisonobe, T., et al. Diagnostic value of markers of muscle degeneration in sporadic inclusion body myositis. Acta Myol 30 (2011), 103–108.
    • (2011) Acta Myol , vol.30 , pp. 103-108
    • Dubourg, O.1    Wanschitz, J.2    Maisonobe, T.3
  • 12
    • 84899544973 scopus 로고    scopus 로고
    • A retrospective cohort study identifying the principal pathological features useful in the diagnosis of inclusion body myositis
    • [12] Brady, S., Squier, W., Sewry, C., et al. A retrospective cohort study identifying the principal pathological features useful in the diagnosis of inclusion body myositis. BMJ Open, 4, 2014, e004552.
    • (2014) BMJ Open , vol.4 , pp. e004552
    • Brady, S.1    Squier, W.2    Sewry, C.3
  • 13
    • 66449114033 scopus 로고    scopus 로고
    • p62 at the crossroads of autophagy, apoptosis, and cancer
    • [13] Moscat, J., Diaz-Meco, M.T., p62 at the crossroads of autophagy, apoptosis, and cancer. Cell 137 (2009), 1001–1004.
    • (2009) Cell , vol.137 , pp. 1001-1004
    • Moscat, J.1    Diaz-Meco, M.T.2
  • 14
    • 77956410115 scopus 로고    scopus 로고
    • Selective autophagy: ubiquitin-mediated recognition and beyond
    • [14] Kraft, C., Peter, M., Hofmann, K., Selective autophagy: ubiquitin-mediated recognition and beyond. Nat Cell Biol 12 (2010), 836–841.
    • (2010) Nat Cell Biol , vol.12 , pp. 836-841
    • Kraft, C.1    Peter, M.2    Hofmann, K.3
  • 15
    • 82455172117 scopus 로고    scopus 로고
    • Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins
    • [15] Matsumoto, G., Wada, K., Okuno, M., et al. Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins. Mol Cell 44 (2011), 279–289.
    • (2011) Mol Cell , vol.44 , pp. 279-289
    • Matsumoto, G.1    Wada, K.2    Okuno, M.3
  • 16
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • [16] Venkatraman, P., Wetzel, R., Tanaka, M., et al. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol Cell 14 (2004), 95–104.
    • (2004) Mol Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3
  • 17
    • 38349114036 scopus 로고    scopus 로고
    • Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases
    • [17] Tan, J.M., Wong, E.S., Kirkpatrick, D.S., et al. Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases. Hum Mol Genet 17 (2008), 431–439.
    • (2008) Hum Mol Genet , vol.17 , pp. 431-439
    • Tan, J.M.1    Wong, E.S.2    Kirkpatrick, D.S.3
  • 18
    • 42049100859 scopus 로고    scopus 로고
    • Essential role of sequestosome 1/p62 in regulating accumulation of Lys63-ubiquitinated proteins
    • [18] Wooten, M.W., Geetha, T., Babu, J.R., et al. Essential role of sequestosome 1/p62 in regulating accumulation of Lys63-ubiquitinated proteins. J Biol Chem 283 (2008), 6783–6789.
    • (2008) J Biol Chem , vol.283 , pp. 6783-6789
    • Wooten, M.W.1    Geetha, T.2    Babu, J.R.3
  • 19
    • 34548259958 scopus 로고    scopus 로고
    • p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • [19] Pankiv, S., Clausen, T.H., Lamark, T., et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem 282 (2007), 24131–24145.
    • (2007) J Biol Chem , vol.282 , pp. 24131-24145
    • Pankiv, S.1    Clausen, T.H.2    Lamark, T.3
  • 20
    • 84888431952 scopus 로고    scopus 로고
    • 188th ENMC International Workshop: inclusion body myositis, 2–4 December 2011, Naarden, The Netherlands
    • [20] Rose, M.R., ENMC IBM Working Group. 188th ENMC International Workshop: inclusion body myositis, 2–4 December 2011, Naarden, The Netherlands. Neuromuscul Disord 23 (2013), 1044–1055.
    • (2013) Neuromuscul Disord , vol.23 , pp. 1044-1055
    • Rose, M.R.1
  • 21
    • 79954525564 scopus 로고    scopus 로고
    • Myofibrillar myopathies
    • [21] Selcen, D., Engel, A.G., Myofibrillar myopathies. Handb Clin Neurol 101 (2011), 143–154.
    • (2011) Handb Clin Neurol , vol.101 , pp. 143-154
    • Selcen, D.1    Engel, A.G.2
  • 22
    • 63049101044 scopus 로고    scopus 로고
    • Regulatory ubiquitylation in response to DNA double-strand breaks
    • [22] Panier, S., Durocher, D., Regulatory ubiquitylation in response to DNA double-strand breaks. DNA Repair (Amst) 8 (2009), 436–443.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 436-443
    • Panier, S.1    Durocher, D.2
  • 23
    • 65649128660 scopus 로고    scopus 로고
    • K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway
    • [23] Lauwers, E., Jacob, C., André, B., K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway. J Cell Biol 185 (2009), 493–502.
    • (2009) J Cell Biol , vol.185 , pp. 493-502
    • Lauwers, E.1    Jacob, C.2    André, B.3
  • 24
    • 79955476784 scopus 로고    scopus 로고
    • Myonuclear breakdown in sporadic inclusion body myositis is accompanied by DNA double strand breaks
    • [24] Nishii, M., Nakano, S., Nakamura, S., et al. Myonuclear breakdown in sporadic inclusion body myositis is accompanied by DNA double strand breaks. Neuromuscul Disord 21 (2011), 345–352.
    • (2011) Neuromuscul Disord , vol.21 , pp. 345-352
    • Nishii, M.1    Nakano, S.2    Nakamura, S.3
  • 25
    • 84865191062 scopus 로고    scopus 로고
    • Ubiquilin-1 regulates amyloid precursor protein maturation and degradation by stimulating K63-linked polyubiquitination of lysine 688
    • [25] El Ayadi, A., Stieren, E.S., Barral, J.M., et al. Ubiquilin-1 regulates amyloid precursor protein maturation and degradation by stimulating K63-linked polyubiquitination of lysine 688. Proc Natl Acad Sci USA 109 (2012), 13416–13421.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 13416-13421
    • El Ayadi, A.1    Stieren, E.S.2    Barral, J.M.3
  • 26
    • 0027444952 scopus 로고
    • Beta-amyloid precursor epitopes in muscle fibers of inclusion body myositis
    • [26] Askanas, V., Alvarez, R.B., Engel, W.K., Beta-amyloid precursor epitopes in muscle fibers of inclusion body myositis. Ann Neurol 34 (1993), 551–560.
    • (1993) Ann Neurol , vol.34 , pp. 551-560
    • Askanas, V.1    Alvarez, R.B.2    Engel, W.K.3
  • 27
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • [27] Watts, G.D., Wymer, J., Kovach, M.J., et al. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat Genet 36 (2004), 377–381.
    • (2004) Nat Genet , vol.36 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3
  • 28
    • 84857041474 scopus 로고    scopus 로고
    • Characterization of the Asian myopathy patients with VCP mutations
    • [28] Shi, Z., Hayashi, Y.K., Mitsuhashi, S., et al. Characterization of the Asian myopathy patients with VCP mutations. Eur J Neurol 19 (2012), 501–509.
    • (2012) Eur J Neurol , vol.19 , pp. 501-509
    • Shi, Z.1    Hayashi, Y.K.2    Mitsuhashi, S.3
  • 29
    • 74049124412 scopus 로고    scopus 로고
    • Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease
    • [29] Ju, J.S., Fuentealba, R.A., Miller, S.E., et al. Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease. J Cell Biol 187 (2009), 875–888.
    • (2009) J Cell Biol , vol.187 , pp. 875-888
    • Ju, J.S.1    Fuentealba, R.A.2    Miller, S.E.3
  • 30
    • 53149138951 scopus 로고    scopus 로고
    • TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia
    • [30] Weihl, C.C., Temiz, P., Miller, S.E., et al. TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia. J Neurol Neurosurg Psychiatry 79 (2008), 1186–1189.
    • (2008) J Neurol Neurosurg Psychiatry , vol.79 , pp. 1186-1189
    • Weihl, C.C.1    Temiz, P.2    Miller, S.E.3
  • 31
    • 67650264666 scopus 로고    scopus 로고
    • Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis
    • [31] Salajegheh, M., Pinkus, J.L., Taylor, J.P., et al. Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis. Muscle Nerve 40 (2009), 19–31.
    • (2009) Muscle Nerve , vol.40 , pp. 19-31
    • Salajegheh, M.1    Pinkus, J.L.2    Taylor, J.P.3
  • 32
    • 65349175153 scopus 로고    scopus 로고
    • TAR DNA-binding protein 43 accumulation in protein aggregate myopathies
    • [32] Olivé, M., Janué, A., Moreno, D., et al. TAR DNA-binding protein 43 accumulation in protein aggregate myopathies. J Neuropathol Exp Neurol 68 (2009), 262–273.
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 262-273
    • Olivé, M.1    Janué, A.2    Moreno, D.3
  • 33
    • 77952533111 scopus 로고    scopus 로고
    • VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD
    • [33] Tresse, E., Salomons, F.A., Vesa, J., et al. VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD. Autophagy 6 (2010), 217–227.
    • (2010) Autophagy , vol.6 , pp. 217-227
    • Tresse, E.1    Salomons, F.A.2    Vesa, J.3
  • 34
    • 84876499456 scopus 로고    scopus 로고
    • Cytosolic 5'-nucleotidase 1A autoimmunity in sporadic inclusion body myositis
    • [34] Larman, H.B., Salajegheh, M., Nazareno, R., et al. Cytosolic 5'-nucleotidase 1A autoimmunity in sporadic inclusion body myositis. Ann Neurol 73 (2013), 408–418.
    • (2013) Ann Neurol , vol.73 , pp. 408-418
    • Larman, H.B.1    Salajegheh, M.2    Nazareno, R.3
  • 35
    • 84876491405 scopus 로고    scopus 로고
    • Autoantibodies to cytosolic 5'-nucleotidase 1A in inclusion body myositis
    • [35] Pluk, H., van Hoeve, B.J., van Dooren, S.H., et al. Autoantibodies to cytosolic 5'-nucleotidase 1A in inclusion body myositis. Ann Neurol 73 (2013), 397–407.
    • (2013) Ann Neurol , vol.73 , pp. 397-407
    • Pluk, H.1    van Hoeve, B.J.2    van Dooren, S.H.3
  • 36
    • 84887859867 scopus 로고    scopus 로고
    • The functional logic of cytosolic 5'-nucleotidases
    • [36] Ipata, P.L., Balestri, F., The functional logic of cytosolic 5'-nucleotidases. Curr Med Chem 20 (2013), 4205–4216.
    • (2013) Curr Med Chem , vol.20 , pp. 4205-4216
    • Ipata, P.L.1    Balestri, F.2
  • 37
    • 80053411075 scopus 로고    scopus 로고
    • Suppression of 5'-nucleotidase enzymes promotes AMP-activated protein kinase (AMPK) phosphorylation and metabolism in human and mouse skeletal muscle
    • [37] Kulkarni, S.S., Karlsson, H.K., Szekeres, F., et al. Suppression of 5'-nucleotidase enzymes promotes AMP-activated protein kinase (AMPK) phosphorylation and metabolism in human and mouse skeletal muscle. J Biol Chem 286 (2011), 34567–34574.
    • (2011) J Biol Chem , vol.286 , pp. 34567-34574
    • Kulkarni, S.S.1    Karlsson, H.K.2    Szekeres, F.3
  • 38
    • 84856800302 scopus 로고    scopus 로고
    • Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks
    • [38] Alers, S., Löffler, A.S., Wesselborg, S., et al. Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks. Mol Cell Biol 32 (2012), 2–11.
    • (2012) Mol Cell Biol , vol.32 , pp. 2-11
    • Alers, S.1    Löffler, A.S.2    Wesselborg, S.3
  • 39
    • 20644440418 scopus 로고    scopus 로고
    • The kinase domain of titin controls muscle gene expression and protein turnover
    • [39] Lange, S., Xiang, F., Yakovenko, A., et al. The kinase domain of titin controls muscle gene expression and protein turnover. Science 308 (2005), 1599–1603.
    • (2005) Science , vol.308 , pp. 1599-1603
    • Lange, S.1    Xiang, F.2    Yakovenko, A.3


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