ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structural insight into M-band assembly and mechanics from the titin-obscurin-like-1 complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 68 citations in OpenAlex.
- Solution NMR study of the titin I-band IgI domain I82 shows unusual conformational dynamics.Journal of biomolecular NMR · 2026Article
- Mending the Achilles heels of titin in cardiac and musculoskeletal disease.Biophysical reviews · 2026Review
- An overview of insights and updates on TTN mutations in cardiomyopathies.Frontiers in pharmacology · 2025Review
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
- The role of the M-band myomesin proteins in muscle integrity and cardiac disease.Journal of biomedical science · 2022Review
- Nanosurgical Manipulation of Titin and Its M-Complex.Nanomaterials (Basel, Switzerland) · 2022Article
- In Vitro Fertilization Using Preimplantation Genetic Testing in a Romanian Couple Carrier of Mutations in the TTN Gene: A Case Report and Literature Review.Diagnostics (Basel, Switzerland) · 2021Article
- Making sense of missense variants in TTN-related congenital myopathies.Acta neuropathologica · 2021Article
- Mechanisms ofJournal of cardiovascular development and disease · 2021Review
- The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020Review
- Real-time visualization of titin dynamics reveals extensive reversible photobleaching in human induced pluripotent stem cell-derived cardiomyocytes.American journal of physiology. Cell physiology · 2020Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Obscurin is a semi-flexible molecule in solution.Protein science : a publication of the Protein Society · 2019Article
- Murine obscurin and Obsl1 have functionally redundant roles in sarcolemmal integrity, sarcoplasmic reticulum organization, and muscle metabolism.Communications biology · 2019Article
- Structural diversity in the atomic resolution 3D fingerprint of the titin M-band segment.PloS one · 2019Article
- Obscurin variants and inherited cardiomyopathies.Biophysical reviews · 2017Review
- α-Actinin/titin interaction: A dynamic and mechanically stable cluster of bonds in the muscle Z-disk.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Binding of Myomesin to Obscurin-Like-1 at the Muscle M-Band Provides a Strategy for Isoform-Specific Mechanical Protection.Structure (London, England : 1993) · 2017Article
- A novel FLNC frameshift and an OBSCN variant in a family with distal muscular dystrophy.PloS one · 2017Article
- Exercise-induced alterations and loss of sarcomeric M-line organization in the diaphragm muscle of obscurin knockout mice.American journal of physiology. Cell physiology · 2017Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
In the sarcomeric M-band, the giant ruler proteins titin and obscurin, its small homologue obscurin-like-1 (obsl1), and the myosin cross-linking protein myomesin form a ternary complex that is crucial for the function of the M-band as a mechanical link. Mutations in the last titin immunoglobulin (Ig) domain M10, which interacts with the N-terminal Ig-domains of obscurin and obsl1, lead to hereditary muscle diseases. The M10 domain is unusual not only in that it is a frequent target of disease-linked mutations, but also in that it is the only currently known muscle Ig-domain that interacts with two ligands--obscurin and obsl1--in different sarcomeric subregions. Using x-ray crystallography, we show the structural basis for titin M10 interaction with obsl1 in a novel antiparallel Ig-Ig architecture and unravel the molecular basis of titin-M10 linked myopathies. The severity of these pathologies correlates with the disruption of the titin-obsl1/obscurin complex. Conserved signature residues at the interface account for differences in affinity that direct the cellular sorting in cardiomyocytes. By engineering the interface signature residues of obsl1 to obscurin, and vice versa, their affinity for titin can be modulated similar to the native proteins. In single-molecule force-spectroscopy experiments, both complexes yield at forces of around 30 pN, much lower than those observed for the mechanically stable Z-disk complex of titin and telethonin, suggesting why even moderate weakening of the obsl1/obscurin-titin links has severe consequences for normal muscle functions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.