ArticleThe Journal of biological chemistry2012
Spontaneous dimerization of titin protein Z1Z2 domains induces strong nanomechanical anchoring.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
- Article
- Microbial production of megadalton titin yields fibers with advantageous mechanical properties.Nature communications · 2021Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- The force-dependent mechanism of DnaK-mediated mechanical folding.Science advances · 2018Article
- 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
- Biophysical characterization of naturally occurring titin M10 mutations.Protein science : a publication of the Protein Society · 2015Article
- Domain-domain interactions in filamin A (16-23) impose a hierarchy of unfolding forces.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Muscle elasticity strongly relies on the mechanical anchoring of the giant protein titin to both the sarcomere M-band and the Z-disk. Such strong attachment ensures the reversible dynamics of the stretching-relaxing cycles determining the muscle passive elasticity. Similarly, the design of biomaterials with enhanced elastic function requires experimental strategies able to secure the constituent molecules to avoid mechanical failure. Here we show that an engineered titin-mimicking protein is able to spontaneously dimerize in solution. Our observations reveal that the titin Z1Z2 domains are key to induce dimerization over a long-range distance in proteins that would otherwise remain in their monomeric form. Using single molecule force spectroscopy, we measure the threshold force that triggers the noncovalent transition from protein dimer to monomer, occurring at ∼700 piconewtons. Such extremely high mechanical stability is likely to be a natural protective mechanism that guarantees muscle integrity. We propose a simple molecular model to understand the force-induced dimer-to-monomer transition based on the geometric distribution of forces occurring within a dimeric protein under mechanical tension.
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Registered trials
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