ArticleNature communications2024
Structural domain in the Titin N2B-us region binds to FHL2 in a force-activation dependent manner.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- FHL2 production enabled new insight into its flexibility and unexpected binding stoichiometry with β-catenin.Journal of structural biology: X · 2026Article
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Mending the Achilles heels of titin in cardiac and musculoskeletal disease.Biophysical reviews · 2026Review
- A titin missense variant drives atrial electrical remodeling and is associated with atrial fibrillation.eLife · 2026Article
- Comparative genomics reveals evolutionary signatures of genes associated with jumping in beetles.Zoological research · 2026Article
- A titin missense variant drives atrial electrical remodeling and is associated with atrial fibrillation.medRxiv : the preprint server for health sciences · 2025Article
- Mechanically knocking out titin reveals protein tension loss as a trigger of muscle disease.Nature biomedical engineering · 2025Article
- Theoretical analysis of power-law stress relaxation and calcium-dependent passive mechanics in cardiac muscle.The Journal of physiology · 2025Article
- GSK3β-driven phosphorylation of ABLIM1 regulates its interactions with titin cardiac muscle.The Journal of general physiology · 2025Article
- Decoding force-transmission linkages for therapeutic targeting and engineering.APL bioengineering · 2025Review
- Unlocking the secrets of Cardiac development and function: the critical role of FHL2.Molecular and cellular biochemistry · 2025Review
- TTN:c.12478del in proximal I-band of titin represents a common molecular cause of dilated cardiomyopathy in Slovenian patients.Orphanet journal of rare diseases · 2025Article
- Principles and regulation of mechanosensing.Journal of cell science · 2024Review
- Structural domain in the Titin N2B-us region binds to FHL2 in a force-activation dependent manner.Nature communications · 2024Article
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Authors and funding
5 authors.
Funding
Abstract
Titin N2B unique sequence (N2B-us) is a 572 amino acid sequence that acts as an elastic spring to regulate muscle passive elasticity. It is thought to lack stable tertiary structures and is a force-bearing region that is regulated by mechanical stretching. In this study, the conformation of N2B-us and its interaction with four-and-a-half LIM domain protein 2 (FHL2) are investigated using AlphaFold2 predictions and single-molecule experimental validation. Surprisingly, a stable alpha/beta structural domain is predicted and confirmed in N2B-us that can be mechanically unfolded at forces of a few piconewtons. Additionally, more than twenty FHL2 LIM domain binding sites are predicted to spread throughout N2B-us. Single-molecule manipulation experiments reveals the force-dependent binding of FHL2 to the N2B-us structural domain. These findings provide insights into the mechano-sensing functions of N2B-us and its interactions with FHL2.
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