ArticleProceedings of the National Academy of Sciences of the United States of America2017
α-Actinin/titin interaction: A dynamic and mechanically stable cluster of bonds in the muscle Z-disk.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. 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, 48 citations in OpenAlex.
- Using iPALM to determine protein organisation in cardiac muscle Z-discs.PLoS computational biology · 2026Article
- Mending the Achilles heels of titin in cardiac and musculoskeletal disease.Biophysical reviews · 2026Review
- Cytokine Profiles and Inflammatory Implications in Chagas Disease: Associations with Ventricular Function and Conduction Disorders.Medical sciences (Basel, Switzerland) · 2025Article
- Mechanically weak and highly dynamic state of mechanosensitive titin Ig domains induced by proline isomerization.Nature communications · 2025Article
- Clinical and imaging spectrum of non-congenital dominant ACTN2 myopathy.Journal of neurology · 2025Article
- Protein-extending ACTN2 frameshift variants cause variable myopathy phenotypes by protein aggregation.Annals of clinical and translational neurology · 2024Article
- Multi-domain interaction mediated strength-building in human α-actinin dimers unveiled by direct single-molecule quantification.Nature communications · 2024Article
- TTN truncation variants produce sarcomere-integrating proteins of uncertain functional significance.The Journal of clinical investigation · 2024Article
- Titin: roles in cardiac function and diseases.Frontiers in physiology · 2024Review
- Disruption of Z-Disc Function Promotes Mechanical Dysfunction in Human Myocardium: Evidence for a Dual Myofilament Modulatory Role by Alpha-Actinin 2.International journal of molecular sciences · 2023Article
- Nucleus Mechanosensing in Cardiomyocytes.International journal of molecular sciences · 2023Review
- Molecular basis of interactions between CaMKII and α-actinin-2 that underlie dendritic spine enlargement.eLife · 2023Article
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
- Mutation update for the ACTN2 gene.Human mutation · 2022Review
- Sarcomere maturation: function acquisition, molecular mechanism, and interplay with other organelles.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022Review
- Contributions of Titin and Collagen to Passive Stress in Muscles fromInternational journal of molecular sciences · 2022Article
- Active unfolding of the glucocorticoid receptor by the Hsp70/Hsp40 chaperone system in single-molecule mechanical experiments.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Nano-Precision Tweezers for Mechanosensitive Proteins and Beyond.Molecules and cells · 2022Review
- Myocardial fibrosis reversion via rhACE2-electrospun fibrous patch for ventricular remodeling prevention.NPJ Regenerative medicine · 2021Article
- Actinin BioID reveals sarcomere crosstalk with oxidative metabolism through interactions with IGF2BP2.Cell reports · 2021Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
Abstract
Stable anchoring of titin within the muscle Z-disk is essential for preserving muscle integrity during passive stretching. One of the main candidates for anchoring titin in the Z-disk is the actin cross-linker α-actinin. The calmodulin-like domain of α-actinin binds to the Z-repeats of titin. However, the mechanical and kinetic properties of this important interaction are still unknown. Here, we use a dual-beam optical tweezers assay to study the mechanics of this interaction at the single-molecule level. A single interaction of α-actinin and titin turns out to be surprisingly weak if force is applied. Depending on the direction of force application, the unbinding forces can more than triple. Our results suggest a model where multiple α-actinin/Z-repeat interactions cooperate to ensure long-term stable titin anchoring while allowing the individual components to exchange dynamically.
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Registered trials
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.