ArticleThe Journal of cell biology1995
Studies of the interaction between titin and myosin.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 122 citations in OpenAlex.
- Four New Muscle Myosin II Binding Properties of Titin: Implications for Myofibrillogenesis.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Titin's P-zone domains A164-167 are essential for thick filament structural arrangement.The Journal of general physiology · 2026Article
- Article
- Molecular insights into titin's A-band.Journal of muscle research and cell motility · 2023Article
- Article
- Reading Frame Repair ofCirculation · 2022Article
- Natural variant frequencies across domains from different sarcomere proteins cross-correlate to identify inter-protein contacts associated with cardiac muscle function and disease.Molecular biomedicine · 2021Article
- The Axial Alignment of Titin on the Muscle Thick Filament Supports Its Role as a Molecular Ruler.Journal of molecular biology · 2020Article
- Calcium-dependent titin-thin filament interactions in muscle: observations and theory.Journal of muscle research and cell motility · 2020Review
- Protein arginylation of cytoskeletal proteins in the muscle: modifications modifying function.American journal of physiology. Cell physiology · 2019Review
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
- Hypertrophic cardiomyopathy and the myosin mesa: viewing an old disease in a new light.Biophysical reviews · 2018Review
- Overview of the Muscle Cytoskeleton.Comprehensive Physiology · 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
- Reduced passive force in skeletal muscles lacking protein arginylation.American journal of physiology. Cell physiology · 2016Article
- Skip residues modulate the structural properties of the myosin rod and guide thick filament assembly.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Heavy and light roles: myosin in the morphogenesis of the heart.Cellular and molecular life sciences : CMLS · 2013Review
- Article
- Effects of pathogenic proline mutations on myosin assembly.Journal of molecular biology · 2012Article
- Biochemistry of smooth muscle myosin light chain kinase.Archives of biochemistry and biophysics · 2011Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction of titin with myosin has been studied by binding assays and electron microscopy. Electron micrographs of the titin-myosin complex suggest a binding site near the tip of the tail of the myosin molecule. The distance from the myosin head-tail junction to titin indicates binding 20-30 nm from the myosin COOH terminus. Consistent with this, micrographs of titin-light meromyosin (LMM) show binding near the end of the LMM molecule. Plots of myosin- and LMM-attachment positions along the titin molecule show binding predominantly in the region located in the A band in situ, which is consistent with the proposal that titin regulates thick filament assembly. Estimates of the apparent dissociation constant of the titin-LMM complex were approximately 20 nM. Assays of LMM cyanogen bromide fragments also suggested a strong binding site near the COOH terminus. Proteolysis of a COOH-terminal 17.6-kD CNBr fragment isolated from whole myosin resulted in eight peptides of which only one, comprising 17 residues, bound strongly to titin. Two isoforms of this peptide were detected by protein sequencing. Similar binding data were obtained using synthetic versions of both isoforms. The peptide is located immediately COOH-terminal of the fourth "skip" residue in the myosin tail, which is consistent with the electron microscopy. Skip-4 may have a role in determining thick filament structure, by allowing abrupt bending of the myosin tail close to the titin-binding site.
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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.