Copyright © 2011 Ralph Knöll et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

1. P. K. Luther, “Three-dimensional reconstruction of a simple Z-band in fish muscle,” Journal of Cell Biology, vol. 113, no. 5, pp. 1043–1055, 1991. View at Scopus
2. P. Zou, N. Pinotsis, S. Lange et al., “Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk,” Nature, vol. 439, no. 7073, pp. 229–233, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
3. P. K. Luther, J. S. Barry, and J. M. Squire, “The three-dimensional structure of a vertebrate wide (slow muscle) Z-band: lessons on Z-band assembly,” Journal of Molecular Biology, vol. 315, no. 1, pp. 9–20, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
4. P. K. Luther, “The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling,” Journal of Muscle Research and Cell Motility, vol. 30, no. 5-6, pp. 171–185, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
5. J. M. Squire, H. A. Al-Khayat, C. Knupp, and P. K. Luther, “Molecular architecture in muscle contractile assemblies,” Advances in Protein Chemistry, vol. 71, pp. 17–87, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
6. K. A. Clark, A. S. McElhinny, M. C. Beckerle, and C. C. Gregorio, “Striated muscle cytoarchitecture: an intricate web of form and function,” Annual Review of Cell and Developmental Biology, vol. 18, pp. 637–706, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
7. D. Frank and N. Frey, “Cardiac Z-disc signaling network,” The Journal of Biological Chemistry, vol. 286, pp. 9897–9904, 2011. View at Publisher · View at Google Scholar · View at PubMed
8. D. Frank, C. Kuhn, H. A. Katus, and N. Frey, “The sarcomeric Z-disc: a nodal point in signalling and disease,” Journal of Molecular Medicine, vol. 84, no. 6, pp. 446–468, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
9. F. Sheikh, M. L. Bang, S. Lange, and J. Chen, “‘Z’eroing in on the role of Cypher in striated muscle function, signaling, and human disease,” Trends in Cardiovascular Medicine, vol. 17, no. 8, pp. 258–262, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
10. P. K. Luther, R. Padron, S. Ritter, R. Craig, and J. M. Squire, “Heterogeneity of Z-band structure within a single muscle sarcomere: implications for sarcomere assembly,” Journal of Molecular Biology, vol. 332, no. 1, pp. 161–169, 2003. View at Publisher · View at Google Scholar · View at Scopus
11. R. W. Rowe, “The ultrastructure of Z disks from white, intermediate, and red fibers of mammalian striated muscles,” Journal of Cell Biology, vol. 57, no. 2, pp. 261–277, 1973. View at Scopus
12. M. A. Goldstein, L. H. Michael, J. P. Schroeter, and R. L. Sass, “Z band dynamics as a function of sarcomere length and the contractile state of muscle,” FASEB Journal, vol. 1, no. 2, pp. 133–142, 1987. View at Scopus
13. M. A. Goldstein, L. H. Michael, J. P. Schroeter, and R. L. Sass, “Structural states in the Z band of skeletal muscle correlate with states of active and passive tension,” Journal of General Physiology, vol. 92, no. 1, pp. 113–119, 1988. View at Scopus
14. M. A. Goldstein, J. P. Schoeter, and R. L. Sass, “Two structural states of the vertebrate Z band,” Electron Microscopy Reviews, vol. 3, no. 2, pp. 227–248, 1990. View at Scopus
15. M. Yamaguchi, M. Izumimoto, R. M. Robson, and M. H. Stromer, “Fine structure of wide and narrow vertebrate muscle Z-lines. A proposed model and computer simulation of Z-line architecture,” Journal of Molecular Biology, vol. 184, no. 4, pp. 621–643, 1985. View at Scopus
16. C. M. Hampton, D. W. Taylor, and K. A. Taylor, “Novel structures for alpha-actinin:F-actin interactions and their implications for actin-membrane attachment and tension sensing in the cytoskeleton,” Journal of Molecular Biology, vol. 368, no. 1, pp. 92–104, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
17. B. Mohapatra, S. Jimenez, J. H. Lin, et al., “Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis,” Molecular Genetics and Metabolism, vol. 80, no. 1-2, pp. 207–215, 2003. View at Publisher · View at Google Scholar
18. J. M. Bos and M. J. Ackerman, “Z-disc genes in hypertrophic cardiomyopathy: stretching the cardiomyopathies?” Journal of the American College of Cardiology, vol. 55, pp. 1136–1138, 2010. View at Publisher · View at Google Scholar · View at PubMed
19. C. Chiu, R. D. Bagnall, J. Ingles et al., “Mutations in alpha-actinin-2 cause hypertrophic cardiomyopathy: a genome-wide analysis,” Journal of the American College of Cardiology, vol. 55, no. 11, pp. 1127–1135, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
20. H. A. Louis, J. D. Pino, K. L. Schmeichel, P. Pomies, and M. C. Beckerle, “Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression,” Journal of Biological Chemistry, vol. 272, no. 43, pp. 27484–27491, 1997. View at Publisher · View at Google Scholar · View at Scopus
21. J. Heineke, H. Ruetten, C. Willenbockel et al., “Attenuation of cardiac remodeling after myocardial infarction by muscle LIM protein-calcineurin signaling at the sarcomeric Z-disc,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 5, pp. 1655–1660, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
22. R. Knöll, M. Hoshijima, H. M. Hoffman et al., “The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy,” Cell, vol. 111, no. 7, pp. 943–955, 2002. View at Publisher · View at Google Scholar · View at Scopus
23. R. Knöll, S. Kostin, S. Klede, et al., “A common MLP (muscle LIM protein) variant is associated with cardiomyopathy,” Circulation Research, vol. 106, pp. 695–704, 2010. View at Publisher · View at Google Scholar · View at PubMed
24. Y. Kong, M. J. Flick, A. J. Kudla, and S. F. Konieczny, “Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD,” Molecular and Cellular Biology, vol. 17, no. 8, pp. 4750–4760, 1997. View at Scopus
25. E. Ehler, R. Horowits, C. Zuppinger et al., “Alterations at the intercalated disk associated with the absence of muscle LIM protein,” Journal of Cell Biology, vol. 153, no. 4, pp. 763–772, 2001. View at Publisher · View at Google Scholar · View at Scopus
26. R. Postel, P. Vakeel, J. Topczewski, R. Knöll, and J. Bakkers, “Zebrafish integrin-linked kinase is required in skeletal muscles for strengthening the integrin-ECM adhesion complex,” Developmental Biology, vol. 318, no. 1, pp. 92–101, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
27. M. J. Flick and S. F. Konieczny, “The muscle regulatory and structural protein MLP is a cytoskeletal binding partner of betaI-spectrin,” Journal of Cell Science, vol. 113, no. 9, pp. 1553–1564, 2000. View at Scopus
28. R. Knöll, G. Iaccarino, G. Tarone, et al., “Towards a re-definition of “cardiac hypertrophy” through a rational characterization of left ventricular phenotypes: a position paper of the Working Group “Myocardial Function” of the ESC,” European Journal of Heart Failure, vol. 13, pp. 811–819, 2011. View at Publisher · View at Google Scholar · View at PubMed
29. B. J. Maron, J. A. Towbin, G. Thiene et al., “Contemporary definitions and classification of the cardiomyopathies: an American heart association scientific statement from the council on clinical cardiology, heart failure and transplantation committee; quality of care and outcomes research and functional genomics and translational biology interdisciplinary working groups; and council on epidemiology and prevention,” Circulation, vol. 113, no. 14, pp. 1807–1816, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
30. V. Papalouka, D. A. Arvanitis, E. Vafiadaki et al., “Muscle Lim protein interacts with cofilin 2 and regulates F-actin dynamics in cardiac and skeletal muscle,” Molecular and Cellular Biology, vol. 29, no. 22, pp. 6046–6058, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
31. S. Arber and P. Caroni, “Specificity of single LIM motifs in targeting and LIM/LIM interactions in situ,” Genes and Development, vol. 10, no. 3, pp. 289–300, 1996. View at Scopus
32. M. P. Gupta, S. A. Samant, S. H. Smith, and S. G. Shroff, “HDAC4 and PCAF bind to cardiac sarcomeres and play a role in regulating myofilament contractile activity,” Journal of Biological Chemistry, vol. 283, no. 15, pp. 10135–10146, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
33. B. Buyandelger, K. E. Ng, S. Miocic, et al., “MLP (muscle LIM protein) as a stress sensor in the heart,” Pflügers Archiv, vol. 462, no. 1, pp. 135–142, 2011. View at Publisher · View at Google Scholar · View at PubMed
34. M. Bertz, M. Wilmanns, and M. Rief, “The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 32, pp. 13307–13310, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
35. O. Mayans, P. F. M. van der Ven, M. Wilm et al., “Structural basis for activation of the titin kinase domain during myofibrillogenesis,” Nature, vol. 395, no. 863, p. 869, 1998.
36. R. S. Haworth, F. Cuello, T. J. Herron et al., “Protein kinase D is a novel mediator of cardiac troponin I phosphorylation and regulates myofilament function,” Circulation Research, vol. 95, no. 11, pp. 1091–1099, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
37. A. Kontrogianni-Konstantopoulos, E. M. Jones, D. B. Van Rossum, and R. J. Bloch, “Obscurin is a ligand for small ankyrin 1 in skeletal muscle,” Molecular Biology of the Cell, vol. 14, no. 3, pp. 1138–1148, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
38. T. Furukawa, Y. Ono, H. Tsuchiya et al., “Specific interaction of the potassium channel beta-subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system,” Journal of Molecular Biology, vol. 313, no. 4, pp. 775–784, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
39. A. Mazzone, P. R. Strege, D. J. Tester et al., “A mutation in telethonin alters Nav1.5 function,” Journal of Biological Chemistry, vol. 283, no. 24, pp. 16537–16544, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
40. R. Zhang, J. Yang, J. Zhu, and X. Xu, “Depletion of zebrafish Tcap leads to muscular dystrophy via disrupting sarcomere-membrane interaction, not sarcomere assembly,” Human Molecular Genetics, vol. 18, no. 21, pp. 4130–4140, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
41. L. F. Tian, H. Y. Li, B. F. Jin et al., “MDM2 interacts with and downregulates a sarcomeric protein, TCAP,” Biochemical and Biophysical Research Communications, vol. 345, no. 1, pp. 355–361, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
42. S. H. Witt, H. Granzier, C. C. Witt, and S. Labeit, “MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: towards understanding MURF-dependent muscle ubiquitination,” Journal of Molecular Biology, vol. 350, no. 4, pp. 713–722, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
43. N. Frey and E. N. Olson, “Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins,” Journal of Biological Chemistry, vol. 277, no. 16, pp. 13998–14004, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
44. G. Nicholas, M. Thomas, B. Langley et al., “Titin-cap associates with, and regulates secretion of, Myostatin,” Journal of Cellular Physiology, vol. 193, no. 1, pp. 120–131, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
45. N. Nakano, H. Hori, M. Abe et al., “Interaction of BMP10 with Tcap may modulate the course of hypertensive cardiac hypertrophy,” American Journal of Physiology, vol. 293, no. 6, pp. H3396–H3403, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
46. K. Mihatsch, M. Nestler, H. P. Saluz, A. Henke, and T. Munder, “Proapoptotic protein Siva binds to the muscle protein telethonin in cardiomyocytes during coxsackieviral infection,” Cardiovascular Research, vol. 81, no. 1, pp. 108–115, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
47. A. Ferreiro, M. Mezmezian, M. Olive et al., “Telethonin-deficiency initially presenting as a congenital muscular dystrophy,” Neuromuscular Disorders, vol. 21, no. 6, pp. 433–438, 2011. View at Publisher · View at Google Scholar · View at PubMed
48. E. S. Moreira, T. J. Wiltshire, G. Faulkner et al., “Limb-girdle muscular dystrophy type 2G is caused by mutations in the gene encoding the sarcomeric protein telethonin,” Nature Genetics, vol. 24, no. 2, pp. 163–166, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
49. M. Olive, A. Shatunov, L. Gonzalez et al., “Transcription-terminating mutation in telethonin causing autosomal recessive muscular dystrophy type 2G in a European patient,” Neuromuscular Disorders, vol. 18, no. 12, pp. 929–933, 2008. View at Publisher · View at Google Scholar · View at PubMed
50. T. Hayashi, T. Arimura, M. Itoh-Satoh et al., “Tcap gene mutations in hypertrophic cardiomyopathy and dilated cardiomyopathy,” Journal of the American College of Cardiology, vol. 44, no. 11, pp. 2192–2201, 2004. View at Publisher · View at Google Scholar · View at PubMed
51. R. Knöll, W. A. Linke, P. Zou, et al., “Telethonin deficiency is associated with maladaptation to biomechanical stress in the mammalian heart,” Circulation Research, vol. 109, no. 7, pp. 758–769, 2011. View at Publisher · View at Google Scholar · View at PubMed
52. A. Lange, S. A. Wickstrom, M. Jakobson, R. Zent, K. Sainio, and R. Fassler, “Integrin-linked kinase is an adaptor with essential functions during mouse development,” Nature, vol. 461, no. 7266, pp. 1002–1006, 2009. View at Publisher · View at Google Scholar · View at PubMed
53. Y. B. Kim, S. Choi, M. C. Choi et al., “Cell adhesion-dependent cofilin serine 3 phosphorylation by the integrin-linked kinase·c-Src complex,” Journal of Biological Chemistry, vol. 283, no. 15, pp. 10089–10096, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
54. R. Knöll, R. Postel, J. Wang et al., “Laminin-alpha4 and integrin-linked kinase mutations cause human cardiomyopathy via simultaneous defects in cardiomyocytes and endothelial cells,” Circulation, vol. 116, no. 5, pp. 515–525, 2007. View at Publisher · View at Google Scholar · View at PubMed
55. M. Brancaccio, S. Guazzone, N. Menini et al., “Melusin is a new muscle-specific interactor for beta(1) integrin cytoplasmic domain,” Journal of Biological Chemistry, vol. 274, no. 41, pp. 29282–29288, 1999. View at Publisher · View at Google Scholar · View at Scopus
56. M. Brancaccio, L. Fratta, A. Notte et al., “Melusin, a muscle-specific integrin beta(1)-interacting protein, is required to prevent cardiac failure in response to chronic pressure overload,” Nature Medicine, vol. 9, no. 1, pp. 68–75, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
57. M. De Acetis, A. Notte, F. Accornero et al., “Cardiac overexpression of melusin protects from dilated cardiomyopathy due to long-standing pressure overload,” Circulation Research, vol. 96, no. 10, pp. 1087–1094, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
58. V. Palumbo, L. Segat, L. Padovan et al., “Melusin gene (ITGB1BP2) nucleotide variations study in hypertensive and cardiopathic patients,” BMC Medical Genetics, vol. 10, article 140, 2009. View at Publisher · View at Google Scholar · View at PubMed
59. N. Frey, J. A. Richardson, and E. N. Olson, “Calsarcins, a novel family of sarcomeric calcineurin-binding proteins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 26, pp. 14632–14637, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
60. N. Frey, T. Barrientos, J. M. Shelton et al., “Mice lacking calsarcin-1 are sensitized to calcineurin signaling and show accelerated cardiomyopathy in response to pathological biomechanical stress,” Nature Medicine, vol. 10, no. 12, pp. 1336–1343, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
61. A. Osio, L. Tan, S. N. Chen et al., “Myozenin 2 is a novel gene for human hypertrophic cardiomyopathy,” Circulation Research, vol. 100, no. 6, pp. 766–768, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
62. N. H. Purcell, D. Darwis, O. F. Bueno, J. M. Muller, R. Schule, and J. D. Molkentin, “Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes,” Molecular and Cellular Biology, vol. 24, no. 3, pp. 1081–1095, 2004. View at Publisher · View at Google Scholar · View at Scopus
63. F. Sheikh, A. Raskin, P. H. Chu et al., “An FHL1-containing complex within the cardiomyocyte sarcomere mediates hypertrophic biomechanical stress responses in mice,” Journal of Clinical Investigation, vol. 118, no. 12, pp. 3870–3880, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
64. C. Windpassinger, B. Schoser, V. Straub et al., “An X-linked myopathy with postural muscle atrophy and generalized hypertrophy, termed XMPMA, is caused by mutations in FHL1,” American Journal of Human Genetics, vol. 82, no. 1, pp. 88–99, 2008. View at Publisher · View at Google Scholar · View at PubMed
65. C. M. Quinzii, T. H. Vu, K. C. Min et al., “X-linked dominant scapuloperoneal myopathy is due to a mutation in the gene encoding four-and-a-half-LIM protein 1,” American Journal of Human Genetics, vol. 82, no. 1, pp. 208–213, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
66. J. Schessl, A. Columbus, Y. Hu et al., “Familial reducing body myopathy with cytoplasmic bodies and rigid spine revisited: identification of a second LIM domain mutation in FHL1,” Neuropediatrics, vol. 41, no. 1, pp. 43–46, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
67. J. Schessl, A. L. Taratuto, C. Sewry et al., “Clinical, histological and genetic characterization of reducing body myopathy caused by mutations in FHL1,” Brain, vol. 132, no. 2, pp. 452–464, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
68. J. Schessl, Y. Zou, M. J. McGrath et al., “Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy,” Journal of Clinical Investigation, vol. 118, no. 3, pp. 904–912, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
69. P. M. Guy, D. A. Kenny, and G. N. Gill, “The PDZ domain of the LIM protein enigma binds to beta-tropomyosin,” Molecular Biology of the Cell, vol. 10, no. 6, pp. 1973–1984, 1999. View at Scopus
70. S. Kuroda, C. Tokunaga, Y. Kiyohara et al., “Protein-protein interaction of zinc finger LIM domains with protein kinase C,” Journal of Biological Chemistry, vol. 271, no. 49, pp. 31029–31032, 1996. View at Publisher · View at Google Scholar · View at Scopus
71. Q. Zhou, P. H. Chu, C. Huang et al., “Ablation of Cypher, a PDZ-LIM domain Z-line protein, causes a severe form of congenital myopathy,” Journal of Cell Biology, vol. 155, no. 3, pp. 605–612, 2001. View at Scopus
72. M. Pashmforoush, P. Pomies, K. L. Peterson et al., “Adult mice deficient in actinin-associated LIM-domain protein reveal a developmental pathway for right ventricular cardiomyopathy,” Nature Medicine, vol. 7, no. 5, pp. 591–597, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
73. H. F. Han and M. C. Beckerle, “The ALP-enigma protein ALP-1 functions in actin filament organization to promote muscle structural integrity in caenorhabditis elegans,” Molecular Biology of the Cell, vol. 20, no. 9, pp. 2361–2370, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
74. H. Cheng, K. Kimura, A. K. Peter et al., “Loss of enigma homolog protein results in dilated cardiomyopathy,” Circulation Research, vol. 107, no. 3, pp. 348–356, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
75. S. Arber, J. J. Hunter, J. Ross Jr. et al., “MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure,” Cell, vol. 88, no. 3, pp. 393–403, 1997. View at Publisher · View at Google Scholar · View at Scopus
76. M. Zheng, H. Cheng, X. Li et al., “Cardiac-specific ablation of Cypher leads to a severe form of dilated cardiomyopathy with premature death,” Human Molecular Genetics, vol. 18, no. 4, pp. 701–713, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
77. C. Huang, Q. Zhou, P. Liang et al., “Characterization and in vivo functional analysis of splice variants of cypher,” Journal of Biological Chemistry, vol. 278, no. 9, pp. 7360–7365, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
78. T. Arimura, T. Hayashi, H. Terada et al., “A Cypher/ZASP mutation associated with dilated cardiomyopathy alters the binding affinity to protein kinase C,” Journal of Biological Chemistry, vol. 279, no. 8, pp. 6746–6752, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
79. M. Vatta, B. Mohapatra, S. Jimenez et al., “Mutations in Cypher/ZASP in patients with dilated cardiomyopathy and left ventricular non-compaction,” Journal of the American College of Cardiology, vol. 42, no. 11, pp. 2014–2027, 2003. View at Publisher · View at Google Scholar · View at Scopus
80. Y. Xing, F. Ichida, T. Matsuoka et al., “Genetic analysis in patients with left ventricular noncompaction and evidence for genetic heterogeneity,” Molecular Genetics and Metabolism, vol. 88, no. 1, pp. 71–77, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
81. D. Selcen and A. G. Engel, “Myofibrillar myopathies,” Handbook of Clinical Neurology, vol. 101, pp. 143–154, 2011. View at Publisher · View at Google Scholar · View at PubMed
82. D. Selcen and A. G. Engel, “Mutations in ZASP define a novel form of muscular dystrophy in humans,” Annals of Neurology, vol. 57, no. 2, pp. 269–276, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
83. M. Zheng, H. Cheng, I. Banerjee, and J. Chen, “ALP/Enigma PDZ-LIM domain proteins in the heart,” Journal of Molecular Cell Biology, vol. 2, no. 2, pp. 96–102, 2010. View at Scopus
84. S. Homma, M. Iwasaki, G. D. Shelton, E. Engvall, J. C. Reed, and S. Takayama, “BAG3 deficiency results in fulminant myopathy and early lethality,” American Journal of Pathology, vol. 169, no. 3, pp. 761–773, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
85. D. Selcen, F. Muntoni, B. K. Burton et al., “Mutation in BAG3 causes severe dominant childhood muscular dystrophy,” Annals of Neurology, vol. 65, no. 1, pp. 83–89, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
86. N. Norton, D. Li, M. J. Rieder et al., “Genome-wide studies of copy number variation and exome sequencing identify rare variants in BAG3 as a cause of dilated cardiomyopathy,” American Journal of Human Genetics, vol. 88, no. 3, pp. 273–282, 2011. View at Publisher · View at Google Scholar · View at PubMed
87. E. Villard, C. Perret, F. Gary, et al., “A genome-wide association study identifies two loci associated with heart failure due to dilated cardiomyopathy,” European Heart Journal, vol. 32, pp. 1065–1076, 2011. View at Publisher · View at Google Scholar · View at PubMed
88. P. von Nandelstadh, R. Souymani, M. Baumann, and O. Carpen, “Analysis of myotilin turnover provides mechanistic insight into the role of myotilinopathy-causing mutations,” Biochemical Journal, vol. 436, no. 1, pp. 113–121, 2011. View at Publisher · View at Google Scholar · View at PubMed
89. F. Bennardini, A. Wrzosek, and M. Chiesi, “Alpha B-Crystallin in cardiac tissue: association with actin and desmin filaments,” Circulation Research, vol. 71, no. 2, pp. 288–294, 1992. View at Scopus
90. I. D. Nicholl and R. A. Quinlan, “Chaperone activity of alpha-crystallins modulates intermediate filament assembly,” EMBO Journal, vol. 13, no. 4, pp. 945–953, 1994. View at Scopus
91. P. Vicart, A. Caron, P. Guicheney et al., “A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy,” Nature Genetics, vol. 20, no. 1, pp. 92–95, 1998. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
92. Q. Zheng, H. Su, M. J. Ranek, and X. Wang, “Autophagy and p62 in cardiac proteinopathy,” Circulation Research, vol. 109, pp. 296–308, 2011. View at Publisher · View at Google Scholar · View at PubMed
93. S. Krief, J. F. Faivre, P. Robert et al., “Identification and characterization of cvHsp. A novel human small stress protein selectively expressed in cardiovascular and insulin-sensitive tissues,” Journal of Biological Chemistry, vol. 274, no. 51, pp. 36592–36600, 1999. View at Publisher · View at Google Scholar · View at Scopus
94. A. Brodehl, I. Martin, T. Gawlowski, I. Stork, J. Gummert, and H. Milting, “The small heat shock proteins cvHSP and α-B-Crystallin are colocalized and interact in human myocardial tissue,” Clinical Research in Cardiology, vol. 99, supplement 1, p. 467, 2010.
95. T. P. Cappola, M. Li, J. He et al., “Common variants in HSPB7 and FRMD4B associated with advanced heart failure,” Circulation, vol. 3, no. 2, pp. 147–154, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
96. S. J. Matkovich, D. J. Van Booven, A. Hindes et al., “Cardiac signaling genes exhibit unexpected sequence diversity in sporadic cardiomyopathy, revealing HSPB7 polymorphisms associated with disease,” Journal of Clinical Investigation, vol. 120, no. 1, pp. 280–289, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
97. K. Stark, U. B. Esslinger, W. Reinhard et al., “Genetic association study identifies HSPB7 as a risk gene for idiopathic dilated cardiomyopathy,” PLoS Genetics, vol. 6, no. 10, article e1001167, 2010. View at Publisher · View at Google Scholar · View at PubMed
98. M. C. Dalakas, A. Dagvadorj, B. Goudeau et al., “Progressive skeletal myopathy, a phenotypic variant of desmin myopathy associated with desmin mutations,” Neuromuscular Disorders, vol. 13, no. 3, pp. 252–258, 2003. View at Publisher · View at Google Scholar · View at Scopus
99. M. C. Dalakas, K. Y. Park, C. Semino-Mora, H. S. Lee, K. Sivakumar, and L. G. Goldfarb, “Desmin myopathy, a skeletal myopathy with cardiomyopathy caused by mutations in the desmin gene,” The New England Journal of Medicine, vol. 342, no. 11, pp. 770–780, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
100. M. C. Walter, P. Reilich, A. Huebner et al., “Scapuloperoneal syndrome type Kaeser and a wide phenotypic spectrum of adult-onset, dominant myopathies are associated with the desmin mutation R350P,” Brain, vol. 130, no. 6, pp. 1485–1496, 2007. View at Publisher · View at Google Scholar · View at PubMed
101. D. Li, T. Tapscoft, O. Gonzalez et al., “Desmin mutation responsible for idiopathic dilated cardiomyopathy,” Circulation, vol. 100, no. 5, pp. 461–464, 1999. View at Scopus
102. B. Klauke, S. Kossmann, A. Gaertner et al., “De novo desmin-mutation N116S is associated with arrhythmogenic right ventricular cardiomyopathy,” Human Molecular Genetics, vol. 19, no. 23, pp. 4595–4607, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
103. E. Otten, A. Asimaki, A. Maass et al., “Desmin mutations as a cause of right ventricular heart failure affect the intercalated disks,” Heart Rhythm, vol. 7, no. 8, pp. 1058–1064, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
104. P. Pruszczyk, A. Kostera-Pruszczyk, A. Shatunov et al., “Restrictive cardiomyopathy with atrioventricular conduction block resulting from a desmin mutation,” International Journal of Cardiology, vol. 117, no. 2, pp. 244–253, 2007. View at Publisher · View at Google Scholar · View at PubMed
105. M. R. G. Taylor, D. Slavov, L. Ku et al., “Prevalence of desmin mutations in dilated cardiomyopathy,” Circulation, vol. 115, no. 10, pp. 1244–1251, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
106. H. Herrmann, H. Bar, L. Kreplak, S. V. Strelkov, and U. Aebi, “Intermediate filaments: from cell architecture to nanomechanics,” Nature Reviews Molecular Cell Biology, vol. 8, no. 7, pp. 562–573, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
107. M. L. Bang, X. Li, R. Littlefield et al., “Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle,” Journal of Cell Biology, vol. 173, no. 6, pp. 905–916, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
108. C. C. Witt, C. Burkart, D. Labeit et al., “Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo,” EMBO Journal, vol. 25, no. 16, pp. 3843–3855, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
109. S. Labeit, C. A. C. Ottenheijm, and H. Granzier, “Nebulin, a major player in muscle health and disease,” FASEB Journal, vol. 25, no. 3, pp. 822–829, 2011. View at Publisher · View at Google Scholar · View at PubMed
110. J. D. Molkentin, J. R. Lu, C. L. Antos et al., “A calcineurin-dependent transcriptional pathway for cardiac hypertrophy,” Cell, vol. 93, no. 2, pp. 215–228, 1998. View at Publisher · View at Google Scholar · View at Scopus
111. A. C. Newton, “Protein kinase C: poised to signal,” American Journal of Physiology, vol. 298, no. 3, pp. 395–402, 2010. View at Publisher · View at Google Scholar · View at PubMed
112. S. L. Robia, J. Ghanta, V. G. Robu, and J. W. Walker, “Localization and kinetics of protein kinase C-epsilon anchoring in cardiac myocytes,” Biophysical Journal, vol. 80, no. 5, pp. 2140–2151, 2001. View at Publisher · View at Google Scholar
113. X. Gu and S. P. Bishop, “Increased protein kinase C and isozyme redistribution in pressure-overload cardiac hypertrophy in the rat,” Circulation Research, vol. 75, no. 5, pp. 926–931, 1994.
114. G. Wu, T. Toyokawa, H. Hahn, and G. W. Dorn II, “Epsilon protein kinase C in pathological myocardial hypertrophy. Analysis by combined transgenic expression of translocation modifiers and Galphaq,” The Journal of Biological Chemistry, vol. 275, Article ID 10.1074/jbc.C000380200, pp. 29927–29930, 2000.
115. Y. Takeishi, P. Ping, R. Bolli, D. L. Kirkpatrick, B. D. Hoit, and R. A. Walsh, “Transgenic overexpression of constitutively active protein kinase C epsilon causes concentric cardiac hypertrophy,” Circulation Research, vol. 86, no. 12, pp. 1218–1223, 2000. View at Scopus
116. M. Iwata, A. Maturana, M. Hoshijima, et al., “PKCepsilon-PKD1 signaling complex at Z-discs plays a pivotal role in the cardiac hypertrophy induced by G-protein coupling receptor agonists,” Biochemical and Biophysical Research Communications, vol. 327, pp. 1105–1113, 2005.
117. R. Arya, V. Kedar, J. R. Hwang et al., “Muscle ring finger protein-1 inhibits PKC{epsilon} activation and prevents cardiomyocyte hypertrophy,” Journal of Cell Biology, vol. 167, no. 6, pp. 1147–1159, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
118. V. Arndt, N. Dick, R. Tawo et al., “Chaperone-assisted selective autophagy is essential for muscle maintenance,” Current Biology, vol. 20, no. 2, pp. 143–148, 2010. View at Publisher · View at Google Scholar · View at PubMed
119. G. Mearini, S. Schlossarek, M. S. Willis, and L. Carrier, “The ubiquitin-proteasome system in cardiac dysfunction,” Biochimica et Biophysica Acta, vol. 1782, no. 12, pp. 749–763, 2008. View at Publisher · View at Google Scholar · View at PubMed
120. M. S. Willis, W. H. D. Townley-Tilson, E. Y. Kang, J. W. Homeister, and C. Patterson, “Sent to destroy: the ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease,” Circulation Research, vol. 106, no. 3, pp. 463–478, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
121. T. Centner, J. Yano, E. Kimura et al., “Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain,” Journal of Molecular Biology, vol. 306, no. 4, pp. 717–726, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
122. J. A. Spencer, S. Eliazer, R. L. Ilaria Jr., J. A. Richardson, and E. N. Olson, “Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein,” Journal of Cell Biology, vol. 150, no. 4, pp. 771–784, 2000. View at Publisher · View at Google Scholar · View at Scopus
123. H. H. Li, V. Kedar, C. Zhang et al., “Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex,” Journal of Clinical Investigation, vol. 114, no. 8, pp. 1058–1071, 2004. View at Publisher · View at Google Scholar · View at Scopus
124. M. S. Willis, C. Ike, L. Li, D. Z. Wang, D. J. Glass, and C. Patterson, “Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo,” Circulation Research, vol. 100, no. 4, pp. 456–459, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
125. S. Labeit, C. H. Kohl, C. C. Witt, D. Labeit, J. Jung, and H. Granzier, “Modulation of muscle atrophy, fatigue and MLC phosphorylation by MuRF1 as indicated by hindlimb suspension studies on MuRF1-KO mice,” Journal of Biomedicine and Biotechnology, vol. 2010, Article ID 693741, 9 pages, 2010. View at Publisher · View at Google Scholar · View at PubMed
126. F. Raynaud, C. Jond-Necand, A. Marcilhac, D. Furst, and Y. Benyamin, “Calpain 1-gamma filamin interaction in muscle cells: a possible in situ regulation by PKC-alpha,” The International Journal of Biochemistry and Cell Biology, vol. 38, no. 3, pp. 404–413, 2006.
127. L. Qi and S. Y. Boateng, “The circadian protein Clock localizes to the sarcomeric Z-disk and is a sensor of myofilament cross-bridge activity in cardiac myocytes,” Biochemical and Biophysical Research Communications, vol. 351, no. 4, pp. 1054–1059, 2006. View at Publisher · View at Google Scholar · View at PubMed
128. S. Y. Boateng, R. J. Belin, D. L. Geenen et al., “Cardiac dysfunction and heart failure are associated with abnormalities in the subcellular distribution and amounts of oligomeric muscle LIM protein,” American Journal of Physiology, vol. 292, no. 1, pp. H259–H269, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
129. S. Y. Boateng, S. E. Senyo, L. Qi, P. H. Goldspink, and B. Russell, “Myocyte remodeling in response to hypertrophic stimuli requires nucleocytoplasmic shuttling of muscle LIM protein,” Journal of Molecular and Cellular Cardiology, vol. 47, no. 4, pp. 426–435, 2009. View at Publisher · View at Google Scholar · View at PubMed
130. S. Vahebi, A. Ota, M. Li et al., “p38-MAPK induced dephosphorylation of alpha-tropomyosin is associated with depression of myocardial sarcomeric tension and ATPase activity,” Circulation Research, vol. 100, no. 3, pp. 408–415, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
131. S. Lange, E. Ehler, and M. Gautel, “From A to Z and back? Multicompartment proteins in the sarcomere,” Trends in Cell Biology, vol. 16, no. 1, pp. 11–18, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus