Autophagy Defects in Skeletal Myopathies

Literature Cited

1. 1. 

   Parzych KR, Klionsky DJ. 2014. An overview of autophagy: morphology, mechanism, and regulation. Antioxid. Redox Signal. 20:460–73
   [Google Scholar]
2. 2. 

   Feng Y, Yao Z, Klionsky DJ 2015. How to control self-digestion: transcriptional, post-transcriptional, and post-translational regulation of autophagy. Trends Cell Biol 25:354–63
   [Google Scholar]
3. 3. 

   Galluzzi L, Baehrecke EH, Ballabio A, Boya P, Bravo-San Pedro JM et al. 2017. Molecular definitions of autophagy and related processes. EMBO J 36:1811–36
   [Google Scholar]
4. 4. 

   Kast DJ, Dominguez R. 2017. The cytoskeleton–autophagy connection. Curr. Biol. 27:R318–26
   [Google Scholar]
5. 5. 

   Dikic I, Elazar Z. 2018. Mechanism and medical implications of mammalian autophagy. Nat. Rev. Mol. Cell Biol. 19:349–64
   [Google Scholar]
6. 6. 

   Danieli A, Martens S. 2018. p62-mediated phase separation at the intersection of the ubiquitin-proteasome system and autophagy. J. Cell Sci. 131:jcs214304
   [Google Scholar]
7. 7. 

   Kalimo H, Savontaus ML, Lang H, Paljarvi L, Sonninen V et al. 1988. X-linked myopathy with excessive autophagy: a new hereditary muscle disease. Ann. Neurol. 23:258–65
   [Google Scholar]
8. 8. 

   Dowling JJ, Moore SA, Kalimo H, Minassian BA 2015. X-linked myopathy with excessive autophagy: a failure of self-eating. Acta Neuropathol 129:383–90
   [Google Scholar]
9. 9. 

   Saraste A, Koskenvuo JW, Airaksinen J, Ramachandran N, Munteanu I et al. 2015. No cardiomyopathy in X-linked myopathy with excessive autophagy. Neuromuscul. Disord. 25:485–87
   [Google Scholar]
10. 10. 

    Munteanu I, Kalimo H, Saraste A, Nishino I, Minassian BA 2017. Cardiac autophagic vacuolation in severe X-linked myopathy with excessive autophagy. Neuromuscul. Disord. 27:185–87
    [Google Scholar]
11. 11. 

    De Bleecker JL, Engel AG, Winkelmann JC 1993. Localization of dystrophin and β-spectrin in vacuolar myopathies. Am. J. Pathol. 143:1200–8
    [Google Scholar]
12. 12. 

    Holton JL, Beesley C, Jackson M, Venner K, Bhardwaj N et al. 2006. Autophagic vacuolar myopathy in twin girls. Neuropathol. Appl. Neurobiol. 32:253–59
    [Google Scholar]
13. 13. 

    Stenzel W, Nishino I, von Moers A, Kadry MA, Glaeser D et al. 2013. Juvenile autophagic vacuolar myopathy—a new entity or variant?. Neuropathol. Appl. Neurobiol. 39:449–53
    [Google Scholar]
14. 14. 

    Ramachandran N, Munteanu I, Wang P, Ruggieri A, Rilstone JJ et al. 2013. VMA21 deficiency prevents vacuolar ATPase assembly and causes autophagic vacuolar myopathy. Acta Neuropathol 125:439–57
    [Google Scholar]
15. 15. 

    Shippey EA, Wagler VD, Collamer AN 2018. Hydroxychloroquine: an old drug with new relevance. Clevel. Clin. J. Med. 85:459–67
    [Google Scholar]
16. 16. 

    Ding HJ, Denniston AK, Rao VK, Gordon C 2016. Hydroxychloroquine-related retinal toxicity. Rheumatology 55:957–67
    [Google Scholar]
17. 17. 

    Lee HS, Daniels BH, Salas E, Bollen AW, Debnath J, Margeta M 2012. Clinical utility of LC3 and p62 immunohistochemistry in diagnosis of drug-induced autophagic vacuolar myopathies: a case–control study. PLOS ONE 7:e36221
    [Google Scholar]
18. 18. 

    Daniels BH, McComb RD, Mobley BC, Gultekin SH, Lee HS, Margeta M 2013. LC3 and p62 as diagnostic markers of drug-induced autophagic vacuolar cardiomyopathy: a study of three cases. Am. J. Surg. Pathol. 37:1014–21
    [Google Scholar]
19. 19. 

    Avina-Zubieta JA, Johnson ES, Suarez-Almazor ME, Russell AS 1995. Incidence of myopathy in patients treated with antimalarials: a report of three cases and a review of the literature. Br. J. Rheumatol. 34:166–70
    [Google Scholar]
20. 20. 

    Casado E, Gratacos J, Tolosa C, Martinez JM, Ojanguren I et al. 2006. Antimalarial myopathy: an underdiagnosed complication? Prospective longitudinal study of 119 patients. Ann. Rheum. Dis. 65:385–90
    [Google Scholar]
21. 21. 

    Kumamoto T, Araki S, Watanabe S, Ikebe N, Fukuhara N 1989. Experimental chloroquine myopathy: morphological and biochemical studies. Eur. Neurol. 29:202–7
    [Google Scholar]
22. 22. 

    Suzuki T, Nakagawa M, Yoshikawa A, Sasagawa N, Yoshimori T et al. 2002. The first molecular evidence that autophagy relates rimmed vacuole formation in chloroquine myopathy. J. Biochem. 131:647–51
    [Google Scholar]
23. 23. 

    Ohkuma S, Poole B. 1978. Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. PNAS 75:3327–31
    [Google Scholar]
24. 24. 

    Stauber WT, Hedge AM, Trout JJ, Schottelius BA 1981. Inhibition of lysosomal function in red and white skeletal muscles by chloroquine. Exp. Neurol. 71:295–306
    [Google Scholar]
25. 25. 

    Yoon YH, Cho KS, Hwang JJ, Lee SJ, Choi JA, Koh JY 2010. Induction of lysosomal dilatation, arrested autophagy, and cell death by chloroquine in cultured ARPE-19 cells. Investig. Ophthalmol. Vis. Sci. 51:6030–37
    [Google Scholar]
26. 26. 

    Lie SO, Schofield B. 1973. Inactivation of lysosomal function in normal cultured human fibroblasts by chloroquine. Biochem. Pharmacol. 22:3109–14
    [Google Scholar]
27. 27. 

    Klionsky DJ, Abdelmohsen K, Abe A, Abedin MJ, Abeliovich H et al. 2016. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy 12:1–222
    [Google Scholar]
28. 28. 

    Sundelin SP, Terman A. 2002. Different effects of chloroquine and hydroxychloroquine on lysosomal function in cultured retinal pigment epithelial cells. APMIS 110:481–89
    [Google Scholar]
29. 29. 

    Radke J, Stenzel W, Goebel HH 2015. Human NCL neuropathology. Biochim. Biophys. Acta Mol. Basis Dis. 1852:2262–66
    [Google Scholar]
30. 30. 

    Cortese A, Tucci A, Piccolo G, Galimberti CA, Fratta P et al. 2014. Novel CLN3 mutation causing autophagic vacuolar myopathy. Neurology 82:2072–76
    [Google Scholar]
31. 31. 

    Licchetta L, Bisulli F, Fietz M, Valentino ML, Morbin M et al. 2015. A novel mutation of CLN3 associated with delayed-classic juvenile ceroid lipofuscinois and autophagic vacuolar myopathy. Eur. J. Med. Genet. 58:540–44
    [Google Scholar]
32. 32. 

    Radke J, Koll R, Gill E, Wiese L, Schulz A et al. 2018. Autophagic vacuolar myopathy is a common feature of CLN3 disease. Ann. Clin. Transl. Neurol. 5:1385–93
    [Google Scholar]
33. 33. 

    Engel AG. 1970. Acid maltase deficiency in adults: studies in four cases of a syndrome which may mimic muscular dystrophy or other myopathies. Brain 93:599–616
    [Google Scholar]
34. 34. 

    Raben N, Takikita S, Pittis MG, Bembi B, Marie SK et al. 2007. Deconstructing Pompe disease by analyzing single muscle fibers: “to see a world in a grain of sand….”. Autophagy 3:546–52
    [Google Scholar]
35. 35. 

    Raben N, Baum R, Schreiner C, Takikita S, Mizushima N et al. 2009. When more is less: Excess and deficiency of autophagy coexist in skeletal muscle in Pompe disease. Autophagy 5:111–13
    [Google Scholar]
36. 36. 

    Carcel-Trullols J, Kovacs AD, Pearce DA 2015. Cell biology of the NCL proteins: what they do and don't do. Biochim. Biophys. Acta Mol. Basis Dis. 1852:2242–55
    [Google Scholar]
37. 37. 

    Vidal-Donet JM, Carcel-Trullols J, Casanova B, Aguado C, Knecht E 2013. Alterations in ROS activity and lysosomal pH account for distinct patterns of macroautophagy in LINCL and JNCL fibroblasts. PLOS ONE 8:e55526
    [Google Scholar]
38. 38. 

    Kohler L, Puertollano R, Raben N 2018. Pompe disease: from basic science to therapy. Neurotherapeutics 15:928–42
    [Google Scholar]
39. 39. 

    Prater SN, Banugaria SG, DeArmey SM, Botha EG, Stege EM et al. 2012. The emerging phenotype of long-term survivors with infantile Pompe disease. Genet. Med. 14:800–10
    [Google Scholar]
40. 40. 

    Chan J, Desai AK, Kazi ZB, Corey K, Austin S et al. 2017. The emerging phenotype of late-onset Pompe disease: a systematic literature review. Mol. Genet. Metab. 120:163–72
    [Google Scholar]
41. 41. 

    Takemura G, Kanamori H, Okada H, Tsujimoto A, Miyazaki N et al. 2017. Ultrastructural aspects of vacuolar degeneration of cardiomyocytes in human endomyocardial biopsies. Cardiovasc. Pathol. 30:64–71
    [Google Scholar]
42. 42. 

    Lagalice L, Pichon J, Gougeon E, Soussi S, Deniaud J et al. 2018. Satellite cells fail to contribute to muscle repair but are functional in Pompe disease (glycogenosis type II). Acta Neuropathol. Commun. 6:116
    [Google Scholar]
43. 43. 

    Schaaf GJ, van Gestel TJM, in ’t Groen SLM, de Jong B, Boomaars B et al. 2018. Satellite cells maintain regenerative capacity but fail to repair disease-associated muscle damage in mice with Pompe disease. Acta Neuropathol. Commun. 6:119
    [Google Scholar]
44. 44. 

    Nascimbeni AC, Fanin M, Angelini C, Sandri M 2015. New pathogenetic mechanisms that link autophagy to Pompe disease. J. Neuromuscul. Dis. 2:Suppl. 1S9
    [Google Scholar]
45. 45. 

    Lieberman AP, Puertollano R, Raben N, Slaugenhaupt S, Walkley SU, Ballabio A 2012. Autophagy in lysosomal storage disorders. Autophagy 8:719–30
    [Google Scholar]
46. 46. 

    Danon MJ, Oh SJ, DiMauro S, Manaligod JR, Eastwood A et al. 1981. Lysosomal glycogen storage disease with normal acid maltase. Neurology 31:51–57
    [Google Scholar]
47. 47. 

    Endo Y, Furuta A, Nishino I 2015. Danon disease: a phenotypic expression of LAMP-2 deficiency. Acta Neuropathol 129:391–98
    [Google Scholar]
48. 48. 

    Rowland TJ, Sweet ME, Mestroni L, Taylor MR 2016. Danon disease—dysregulation of autophagy in a multisystem disorder with cardiomyopathy. J. Cell Sci. 129:2135–43
    [Google Scholar]
49. 49. 

    Nascimbeni AC, Fanin M, Angelini C, Sandri M 2017. Autophagy dysregulation in Danon disease. Cell Death Dis 8:e2565
    [Google Scholar]
50. 50. 

    Furuta A, Wakabayashi K, Haratake J, Kikuchi H, Kabuta T et al. 2013. Lysosomal storage and advanced senescence in the brain of LAMP-2-deficient Danon disease. Acta Neuropathol 125:459–61
    [Google Scholar]
51. 51. 

    Chi C, Leonard A, Knight WE, Beussman KM, Zhao Y et al. 2019. LAMP-2B regulates human cardiomyocyte function by mediating autophagosome–lysosome fusion. PNAS 116:556–65
    [Google Scholar]
52. 52. 

    Finkelstein Y, Aks SE, Hutson JR, Juurlink DN, Nguyen P et al. 2010. Colchicine poisoning: the dark side of an ancient drug. Clin. Toxicol. 48:407–14
    [Google Scholar]
53. 53. 

    Kuncl RW, Duncan G, Watson D, Alderson K, Rogawski MA, Peper M 1987. Colchicine myopathy and neuropathy. N. Engl. J. Med. 316:1562–68
    [Google Scholar]
54. 54. 

    Kwon OC, Hong S, Ghang B, Kim YG, Lee CK, Yoo B 2017. Risk of colchicine-associated myopathy in gout: influence of concomitant use of statin. Am. J. Med. 130:583–87
    [Google Scholar]
55. 55. 

    Fernandez C, Figarella-Branger D, Alla P, Harle JR, Pellissier JF 2002. Colchicine myopathy: a vacuolar myopathy with selective type I muscle fiber involvement. An immunohistochemical and electron microscopic study of two cases. Acta Neuropathol 103:100–6
    [Google Scholar]
56. 56. 

    Kuncl RW. 2009. Agents and mechanisms of toxic myopathy. Curr. Opin. Neurol. 22:506–15
    [Google Scholar]
57. 57. 

    Shinde A, Nakano S, Abe M, Kohara N, Akiguchi I, Shibasaki H 2000. Accumulation of microtubule-based motor protein in a patient with colchicine myopathy. Neurology 55:1414–15
    [Google Scholar]
58. 58. 

    Ju JS, Varadhachary AS, Miller SE, Weihl CC 2010. Quantitation of “autophagic flux” in mature skeletal muscle. Autophagy 6:929–35
    [Google Scholar]
59. 59. 

    Ching JK, Ju JS, Pittman SK, Margeta M, Weihl CC 2013. Increased autophagy accelerates colchicine-induced muscle toxicity. Autophagy 9:2115–25
    [Google Scholar]
60. 60. 

    Kimonis VE, Kovach MJ, Waggoner B, Leal S, Salam A et al. 2000. Clinical and molecular studies in a unique family with autosomal dominant limb-girdle muscular dystrophy and Paget disease of bone. Genet. Med. 2:232–41
    [Google Scholar]
61. 61. 

    Evangelista T, Weihl CC, Kimonis V, Lochmüller H, VCP Related Diseases Consortium 2016. 215th ENMC International Workshop VCP-related multi-system proteinopathy (IBMPFD) 13–15 November 2015, Heemskerk, The Netherlands. Neuromuscul. Disord. 26:535–47
    [Google Scholar]
62. 62. 

    Taylor JP. 2015. Multisystem proteinopathy: intersecting genetics in muscle, bone, and brain degeneration. Neurology 85:658–60
    [Google Scholar]
63. 63. 

    Al-Obeidi E, Al-Tahan S, Surampalli A, Goyal N, Wang AK et al. 2018. Genotype–phenotype study in patients with valosin-containing protein mutations associated with multisystem proteinopathy. Clin. Genet. 93:119–25
    [Google Scholar]
64. 64. 

    Ye Y, Tang WK, Zhang T, Xia D 2017. A mighty “protein extractor” of the cell: structure and function of the p97/CDC48 ATPase. Front. Mol. Biosci. 4:39
    [Google Scholar]
65. 65. 

    Papadopoulos C, Kirchner P, Bug M, Grum D, Koerver L et al. 2017. VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of ruptured lysosomes by autophagy. EMBO J 36:135–50
    [Google Scholar]
66. 66. 

    Johnson AE, Shu H, Hauswirth AG, Tong A, Davis GW 2015. VCP-dependent muscle degeneration is linked to defects in a dynamic tubular lysosomal network in vivo. eLife 4:e07366
    [Google Scholar]
67. 67. 

    Buchan JR, Kolaitis RM, Taylor JP, Parker R 2013. Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function. Cell 153:1461–74
    [Google Scholar]
68. 68. 

    Lee Y, Jonson PH, Sarparanta J, Palmio J, Sarkar M et al. 2018. TIA1 variant drives myodegeneration in multisystem proteinopathy with SQSTM1 mutations. J. Clin. Investig. 128:1164–77
    [Google Scholar]
69. 69. 

    Wang B, Maxwell BA, Joo JH, Gwon Y, Messing J et al. 2019. ULK1 and ULK2 regulate stress granule disassembly through phosphorylation and activation of VCP/p97. Mol. Cell 74:742–57.e8
    [Google Scholar]
70. 70. 

    Batonnet-Pichon S, Behin A, Cabet E, Delort F, Vicart P, Lilienbaum A 2017. Myofibrillar myopathies: new perspectives from animal models to potential therapeutic approaches. J. Neuromuscul. Dis. 4:1–15
    [Google Scholar]
71. 71. 

    Fichna JP, Maruszak A, Zekanowski C 2018. Myofibrillar myopathy in the genomic context. J. Appl. Genet. 59:431–39
    [Google Scholar]
72. 72. 

    Kley RA, van der Ven PF, Olive M, Hohfeld J, Goldfarb LG et al. 2013. Impairment of protein degradation in myofibrillar myopathy caused by FLNC/filamin C mutations. Autophagy 9:422–23
    [Google Scholar]
73. 73. 

    Arndt V, Dick N, Tawo R, Dreiseidler M, Wenzel D et al. 2010. Chaperone-assisted selective autophagy is essential for muscle maintenance. Curr. Biol. 20:143–48
    [Google Scholar]
74. 74. 

    Ulbricht A, Eppler FJ, Tapia VE, van der Ven PF, Hampe N et al. 2013. Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. Curr. Biol. 23:430–35
    [Google Scholar]
75. 75. 

    Bouhy D, Juneja M, Katona I, Holmgren A, Asselbergh B et al. 2018. A knock-in/knock-out mouse model of HSPB8-associated distal hereditary motor neuropathy and myopathy reveals toxic gain-of-function of mutant Hspb8. Acta Neuropathol 135:131–48
    [Google Scholar]
76. 76. 

    Ruparelia AA, Oorschot V, Vaz R, Ramm G, Bryson-Richardson RJ 2014. Zebrafish models of BAG3 myofibrillar myopathy suggest a toxic gain of function leading to BAG3 insufficiency. Acta Neuropathol 128:821–33
    [Google Scholar]
77. 77. 

    Ruparelia AA, Oorschot V, Ramm G, Bryson-Richardson RJ 2016. FLNC myofibrillar myopathy results from impaired autophagy and protein insufficiency. Hum. Mol. Genet. 25:2131–42
    [Google Scholar]
78. 78. 

    Sandell S, Huovinen S, Palmio J, Raheem O, Lindfors M et al. 2016. Diagnostically important muscle pathology in DNAJB6 mutated LGMD1D. Acta Neuropathol. Commun. 4:9
    [Google Scholar]
79. 79. 

    Ghaoui R, Palmio J, Brewer J, Lek M, Needham M et al. 2016. Mutations in HSPB8 causing a new phenotype of distal myopathy and motor neuropathy. Neurology 86:391–98
    [Google Scholar]
80. 80. 

    Weihl CC, Iyadurai S, Baloh RH, Pittman SK, Schmidt RE et al. 2015. Autophagic vacuolar pathology in desminopathies. Neuromuscul. Disord. 25:199–206
    [Google Scholar]
81. 81. 

    Grumati P, Coletto L, Sabatelli P, Cescon M, Angelin A et al. 2010. Autophagy is defective in collagen VI muscular dystrophies, and its reactivation rescues myofiber degeneration. Nat. Med. 16:1313–20
    [Google Scholar]
82. 82. 

    Masiero E, Agatea L, Mammucari C, Blaauw B, Loro E et al. 2009. Autophagy is required to maintain muscle mass. Cell Metab 10:507–15
    [Google Scholar]
83. 83. 

    De Palma C, Morisi F, Cheli S, Pambianco S, Cappello V et al. 2012. Autophagy as a new therapeutic target in Duchenne muscular dystrophy. Cell Death Dis 3:e418
    [Google Scholar]
84. 84. 

    Jungbluth H, Gautel M. 2014. Pathogenic mechanisms in centronuclear myopathies. Front. Aging Neurosci. 6:339
    [Google Scholar]
85. 85. 

    Vergne I, Roberts E, Elmaoued RA, Tosch V, Delgado MA et al. 2009. Control of autophagy initiation by phosphoinositide 3-phosphatase Jumpy. EMBO J 28:2244–58
    [Google Scholar]
86. 86. 

    Al-Qusairi L, Prokic I, Amoasii L, Kretz C, Messaddeq N et al. 2013. Lack of myotubularin (MTM1) leads to muscle hypotrophy through unbalanced regulation of the autophagy and ubiquitin-proteasome pathways. FASEB J 27:3384–94
    [Google Scholar]
87. 87. 

    Fetalvero KM, Yu Y, Goetschkes M, Liang G, Valdez RA et al. 2013. Defective autophagy and mTORC1 signaling in myotubularin null mice. Mol. Cell. Biol. 33:98–110
    [Google Scholar]
88. 88. 

    Durieux AC, Vignaud A, Prudhon B, Viou MT, Beuvin M et al. 2010. A centronuclear myopathy–dynamin 2 mutation impairs skeletal muscle structure and function in mice. Hum. Mol. Genet. 19:4820–36
    [Google Scholar]
89. 89. 

    Durieux AC, Vassilopoulos S, Laine J, Fraysse B, Brinas L et al. 2012. A centronuclear myopathy–dynamin 2 mutation impairs autophagy in mice. Traffic 13:869–79
    [Google Scholar]
90. 90. 

    Nonaka I, Sunohara N, Ishiura S, Satoyoshi E 1981. Familial distal myopathy with rimmed vacuole and lamellar (myeloid) body formation. J. Neurol. Sci. 51:141–55
    [Google Scholar]
91. 91. 

    Argov Z, Yarom R. 1984. “Rimmed vacuole myopathy” sparing the quadriceps: a unique disorder in Iranian Jews. J. Neurol. Sci. 64:33–43
    [Google Scholar]
92. 92. 

    Eisenberg I, Avidan N, Potikha T, Hochner H, Chen M et al. 2001. The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy. Nat. Genet. 29:83–87
    [Google Scholar]
93. 93. 

    Nishino I, Noguchi S, Murayama K, Driss A, Sugie K et al. 2002. Distal myopathy with rimmed vacuoles is allelic to hereditary inclusion body myopathy. Neurology 59:1689–93
    [Google Scholar]
94. 94. 

    Carrillo N, Malicdan MC, Huizing M 2018. GNE myopathy: etiology, diagnosis, and therapeutic challenges. Neurotherapeutics 15:900–14
    [Google Scholar]
95. 95. 

    Nonaka I, Murakami N, Suzuki Y, Kawai M 1998. Distal myopathy with rimmed vacuoles. Neuromuscul. Disord. 8:333–37
    [Google Scholar]
96. 96. 

    Broccolini A, Mirabella M. 2015. Hereditary inclusion-body myopathies. Biochim. Biophys. Acta Mol. Basis Dis. 1852:644–50
    [Google Scholar]
97. 97. 

    Malicdan MC, Noguchi S, Hayashi YK, Nonaka I, Nishino I 2009. Prophylactic treatment with sialic acid metabolites precludes the development of the myopathic phenotype in the DMRV-hIBM mouse model. Nat. Med. 15:690–95
    [Google Scholar]
98. 98. 

    Nogalska A, D'Agostino C, Engel WK, Cacciottolo M, Asada S et al. 2015. Activation of the unfolded protein response in sporadic inclusion-body myositis but not in hereditary GNE inclusion-body myopathy. J. Neuropathol. Exp. Neurol. 74:538–46
    [Google Scholar]
99. 99. 

    Cho A, Christine M, Malicdan V, Miyakawa M, Nonaka I et al. 2017. Sialic acid deficiency is associated with oxidative stress leading to muscle atrophy and weakness in GNE myopathy. Hum. Mol. Genet. 26:3081–93
    [Google Scholar]
100. 100. 

     Keller CW, Schmidt J, Lunemann JD 2017. Immune and myodegenerative pathomechanisms in inclusion body myositis. Ann. Clin. Transl. Neurol. 4:422–45
     [Google Scholar]
101. 101. 

     Jabari D, Vedanarayanan VV, Barohn RJ, Dimachkie MM 2018. Update on inclusion body myositis. Curr. Rheumatol. Rep. 20:52
     [Google Scholar]
102. 102. 

     Hiniker A, Daniels BH, Lee HS, Margeta M 2013. Comparative utility of LC3, p62 and TDP-43 immunohistochemistry in differentiation of inclusion body myositis from polymyositis and related inflammatory myopathies. Acta Neuropathol. Commun. 1:29
     [Google Scholar]
103. 103. 

     Brady S, Squier W, Sewry C, Hanna M, Hilton-Jones D, Holton JL 2014. A retrospective cohort study identifying the principal pathological features useful in the diagnosis of inclusion body myositis. BMJ Open 4:e004552
     [Google Scholar]
104. 104. 

     Lloyd TE, Mammen AL, Amato AA, Weiss MD, Needham M, Greenberg SA 2014. Evaluation and construction of diagnostic criteria for inclusion body myositis. Neurology 83:426–33
     [Google Scholar]
105. 105. 

     Benveniste O, Stenzel W, Hilton-Jones D, Sandri M, Boyer O, van Engelen BG 2015. Amyloid deposits and inflammatory infiltrates in sporadic inclusion body myositis: the inflammatory egg comes before the degenerative chicken. Acta Neuropathol 129:611–24
     [Google Scholar]
106. 106. 

     Weihl CC, Mammen AL. 2017. Sporadic inclusion body myositis—a myodegenerative disease or an inflammatory myopathy. Neuropathol. Appl. Neurobiol. 43:82–91
     [Google Scholar]
107. 107. 

     Hiniker A, Daniels BH, Margeta M 2016. T-cell-mediated inflammatory myopathies in HIV-positive individuals: a histologic study of 19 cases. J. Neuropathol. Exp. Neurol. 75:239–45
     [Google Scholar]
108. 108. 

     Ontaneda D, Thompson AJ, Fox RJ, Cohen JA 2017. Progressive multiple sclerosis: prospects for disease therapy, repair, and restoration of function. Lancet 389:1357–66
     [Google Scholar]
109. 109. 

     Britson KA, Yang SY, Lloyd TE 2018. New developments in the genetics of inclusion body myositis. Curr. Rheumatol. Rep. 20:26
     [Google Scholar]
110. 110. 

     Guttsches AK, Brady S, Krause K, Maerkens A, Uszkoreit J et al. 2017. Proteomics of rimmed vacuoles define new risk allele in inclusion body myositis. Ann. Neurol. 81:227–39
     [Google Scholar]
111. 111. 

     Pankiv S, Alemu EA, Brech A, Bruun JA, Lamark T et al. 2010. FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end–directed vesicle transport. J. Cell Biol. 188:253–69
     [Google Scholar]
112. 112. 

     Castagnaro S, Pellegrini C, Pellegrini M, Chrisam M, Sabatelli P et al. 2016. Autophagy activation in COL6 myopathic patients by a low-protein-diet pilot trial. Autophagy 12:2484–95
     [Google Scholar]
113. 113. 

     Drost MR, Hesselink RP, Oomens CW, van der Vusse GJ 2005. Effects of non-contractile inclusions on mechanical performance of skeletal muscle. J. Biomech. 38:1035–43
     [Google Scholar]
114. 114. 

     Nemazanyy I, Blaauw B, Paolini C, Caillaud C, Protasi F et al. 2013. Defects of Vps15 in skeletal muscles lead to autophagic vacuolar myopathy and lysosomal disease. EMBO Mol. Med. 5:870–90
     [Google Scholar]
115. 115. 

     Spampanato C, Feeney E, Li L, Cardone M, Lim JA et al. 2013. Transcription factor EB (TFEB) is a new therapeutic target for Pompe disease. EMBO Mol. Med. 5:691–706
     [Google Scholar]
116. 116. 

     Tang AH, Rando TA. 2014. Induction of autophagy supports the bioenergetic demands of quiescent muscle stem cell activation. EMBO J 33:2782–97
     [Google Scholar]
117. 117. 

     Hofmann JW, Seeley WW, Huang EJ 2019. RNA binding proteins and the pathogenesis of frontotemporal lobar degeneration. Annu. Rev. Pathol. Mech. Dis. 14:469–95
     [Google Scholar]
118. 118. 

     Ching JK, Elizabeth SV, Ju JS, Lusk C, Pittman SK, Weihl CC 2013. mTOR dysfunction contributes to vacuolar pathology and weakness in valosin-containing protein associated inclusion body myopathy. Hum. Mol. Genet. 22:1167–79
     [Google Scholar]
119. 119. 

     Ching JK, Weihl CC. 2013. Rapamycin-induced autophagy aggravates pathology and weakness in a mouse model of VCP-associated myopathy. Autophagy 9:799–800
     [Google Scholar]
120. 120. 

     Nalbandian A, Llewellyn KJ, Nguyen C, Yazdi PG, Kimonis VE 2015. Rapamycin and chloroquine: The in vitro and in vivo effects of autophagy-modifying drugs show promising results in valosin containing protein multisystem proteinopathy. PLOS ONE 10:e0122888
     [Google Scholar]
121. 121. 

     Ahmed M, Machado PM, Miller A, Spicer C, Herbelin L et al. 2016. Targeting protein homeostasis in sporadic inclusion body myositis. Sci. Transl. Med. 8:331ra41
     [Google Scholar]
122. 122. 

     Sanbe A, Daicho T, Mizutani R, Endo T, Miyauchi N et al. 2009. Protective effect of geranylgera-nylacetone via enhancement of HSPB8 induction in desmin-related cardiomyopathy. PLOS ONE 4:e5351
     [Google Scholar]