The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Loss of Enigma Homolog Protein Results in Dilated Cardiomyopathy
Open accessAbstract
Rationale: The Z-line, alternatively termed the Z-band or Z-disc, is a highly ordered structure at the border between 2 sarcomeres. Enigma subfamily proteins (Enigma, Enigma homolog protein, and Cypher) of the PDZ-LIM domain protein family are Z-line proteins. Among the Enigma subfamily, Cypher has been demonstrated to play a pivotal role in the structure and function of striated muscle, whereas the role of Enigma homolog protein (ENH) in muscle remains largely unknown. Objective: We studied the role of Enigma homolog protein in the heart using global and cardiac-specific ENH knockout mouse models. Methods and Results: We identified new exons and splice isoforms for ENH in the mouse heart. Impaired cardiac contraction and dilated cardiomyopathy were observed in ENH null mice. Mice with cardiac specific ENH deletion developed a similar dilated cardiomyopathy. Like Cypher, ENH interacted with Calsarcin-1, another Z-line protein. Moreover, biochemical studies showed that ENH, Cypher short isoform and Calsarcin-1 are within the same protein complex at the Z-line. Cypher short isoform and Calsarcin-1 proteins are specifically downregulated in ENH null hearts. Conclusions: We have identified an ENH-CypherS-Calsarcin protein complex at the Z-line. Ablation of ENH leads to destabilization of this protein complex and dilated cardiomyopathy.
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“ENH is a family of PDZ-LIM domain proteins that localize to Z-disk and serve as scaffolds for signaling complexes (65).”
From Distinct hypertrophic cardiomyopathy genotypes result in convergent sarcomeric proteoform profiles revealed by top-down proteomics (2020) · cites this paper as [65]
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Cites
Striated Muscle Cytoarchitecture: An Intricate Web of Form and Function
Clark, K. A., McElhinny, A., Beckerle, M. C., & Gregorio, C. C. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.012502.105840 · Cited by 705
Towbin, J. A., & Bowles, N. E. (2002) · Nature · doi:10.1038/415227a · Cited by 542
Mutations in Cypher/ZASPin patients with dilated cardiomyopathy and left ventricular non-compaction
Vatta, M., Mohapatra, B., Jimenez, S., Sánchez, X., Faulkner, G., Perles, Z., Sinagra, G., Lin, J.-H. I., Vu, T. M., Zhou, Q., et al. (2003) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2003.10.021 · Cited by 520
Self-citationCostameres: the Achilles' Heel of Herculean Muscle
Ervasti, J. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.r200021200 · Cited by 447
Transcriptional Regulation During Cardiac Growth and Development
Chien, K. R., Zhu, H., Knowlton, K. U., Miller‐Hance, W. C., van Bilsen, M., O’Brien, T. X., & Evans, S. M. (1993) · Annual Review of Physiology · doi:10.1146/annurev.ph.55.030193.000453 · Cited by 370
Self-citationAn essential role of Bmp4 in the atrioventricular septation of the mouse heart
Jiao, K., Kulessa, H., Tompkins, K., Zhou, Y., Batts, L., Baldwin, H. S., & Hogan, B. L. M. (2003) · Genes & Development · doi:10.1101/gad.1124803 · Cited by 366
Calsarcins, a novel family of sarcomeric calcineurin-binding proteins
Frey, N., Richardson, J. A., & Olson, E. N. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.260501097 · Cited by 303
Filamin 2 (FLN2): A Muscle-specific Sarcoglycan Interacting Protein
Thompson, T. G., Chan, Y.-M. M., Hack, A. A., Brosius, M. A., Rajala, M. W., Lidov, H. G. W., McNally, E. M., Watkins, S. C., & Kunkel, L. M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.1.115 · Cited by 294
Ablation of Cypher, a PDZ-LIM domain Z-line protein, causes a severe form of congenital myopathy
Zhou, Q., Chu, P., Huang, C., Cheng, C., Martone, M. E., Knoll, G., Shelton, G. D., Evans, S. Μ., & Chen, J. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200107092 · Cited by 283
Self-citationProtein-Protein Interaction of Zinc Finger LIM Domains with Protein Kinase C
Kuroda, S., Tokunaga, C., Kiyohara, Y., Higuchi, O., Konishi, H., Mizuno, K., Gill, G. N., & Kikkawa, U. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31029 · Cited by 249
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Bang, C., Bátkai, S., Dangwal, S., Gupta, S. K., Foinquinos, A., Holzmann, A., Just, A., Remke, J., Zimmer, K., Zeug, A., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci70577 · Cited by 995
“This is of interest, as cardiomyocyte-specific PDLIM5 knockout mice develop cardiomyopathy, suggesting PDLIM5 to play a major role in cardiac muscle structure and function (29).”
Overview of the Muscle Cytoskeleton
Henderson, C. A., Gomez, C. G., Novak, S. M., Mi‐Mi, L., & Gregorio, C. C. (2017) · Comprehensive physiology · doi:10.1002/cphy.c160033 · Cited by 333
“Filaments composed of keratin 8 and 19 contribute to linking the contractile apparatus at both the peripheral Zdiscs and M-bands to the sarcolemma (503) (Fig.”
InfluentialThe physiological role of cardiac cytoskeleton and its alterations in heart failure
Sequeira, V., Nijenkamp, L. L. A. M., Regan, J. A., & van der Velden, J. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.07.011 · Cited by 198
Cardiac Z-disc Signaling Network
Frank, D., & Frey, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.174268 · Cited by 188
Cardiac Extracellular Vesicles in Normal and Infarcted Heart
Chistiakov, D. A., Orekhov, A. N., & Bobryshev, Y. V. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17010063 · Cited by 166
“Both miR-21* targets play an important role in organizing cardiac muscle structure and function, and their downregulation results in cardiac hypertrophy [51–53].”
Background
Metadata
- Authors
- Cheng, H., Kimura, K., Peter, A. K., Cui, L., Ouyang, K., Shen, T., Liu, Y., Gu, Y., Dalton, N. D., Evans, S. M., Knowlton, K. U., Peterson, K. L., & Chen, J.
- Affiliations
- University of California San Diego (US)
- From the Department of Medicine, University of California–San Diego, La Jolla, Calif.
- ORCID
- Venue
- Circulation Research
- Published
- 2010-08-06
- Volume
- 107
- Issue
- 3
- Pages
- 348-356
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- PMC
- PMC3684396
- OpenAlex
- W2004101138
- Cited by
- 106
- References
- 45
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 6 · 2023: 5 · 2022: 8 · 2021: 6 · 2020: 8 · 2019: 6 · 2018: 1 · 2017: 6 · 2016: 9 · 2015: 9 · 2014: 6 · 2013: 8 · 2012: 11
- FWCI
- 6.15
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Circulation Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (1r01hl106968-01)
- National Heart, Lung, and Blood Institute (R01-HL106968, P01HL046345, R01HL066100, T32HL007444)
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
- Keywords
- dilated cardiomyopathy, Z-line, Cypher, sarcomere, cardiac contraction, protein complexes, cardiac-specific knockout mice, striated muscle
- MeSH terms
- Animals, Cardiomyopathy, Dilated, Carrier Proteins, Exons, Microfilament Proteins, Muscle Proteins, Myocardial Contraction, Plasmids, Systole, Polymerase Chain Reaction, Alternative Splicing, Mice, Knockout, Homeodomain Proteins, Protein Isoforms, Adaptor Proteins, Signal Transducing, Mice, LIM Domain Proteins
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