ArticleThe Journal of experimental biology2007
Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch.
Article in The Journal of experimental biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 69 citations in OpenAlex.
- Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS.Protein science : a publication of the Protein Society · 2025Article
- The unique biology of catch muscles: insights into structure, function, and robotics innovations.Frontiers in bioengineering and biotechnology · 2025Review
- Article
- Mechanism and Function of the Catch State in Molluscan Smooth Muscle: A Historical Perspective.International journal of molecular sciences · 2020Review
- Transcriptomic analysis ofJournal of nematology · 2020Article
- Passive force enhancement in striated muscle.Journal of applied physiology (Bethesda, Md. : 1985) · 2019Review
- Scalable, Non-denaturing Purification of Phosphoproteins Using GaThe protein journal · 2019Article
- Why are muscles strong, and why do they require little energy in eccentric action?Journal of sport and health science · 2018Article
- Article
- Physiological Mechanisms of Eccentric Contraction and Its Applications: A Role for the Giant Titin Protein.Frontiers in physiology · 2017Review
- Muscle contraction phenotypic analysis enabled by optogenetics reveals functional relationships of sarcomere components in Caenorhabditis elegans.Scientific reports · 2016Article
- Twitchin kinase interacts with MAPKAP kinase 2 in Caenorhabditis elegans striated muscle.Molecular biology of the cell · 2015Article
- Catch muscle myorod modulates ATPase activity of Myosin in a phosphorylation-dependent way.PloS one · 2015Article
- Myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro.Journal of muscle research and cell motility · 2013Article
- Cytoskeletal protein kinases: titin and its relations in mechanosensing.Pflugers Archiv : European journal of physiology · 2011Review
- Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin.Journal of structural biology · 2011Article
- A force-activated kinase in a catch smooth muscle.Journal of muscle research and cell motility · 2011Article
- Myosin binding protein-C: a regulator of actomyosin interaction in striated muscle.Journal of biomedicine & biotechnology · 2011Review
- The N-terminal region of twitchin binds thick and thin contractile filaments: redundant mechanisms of catch force maintenance.The Journal of biological chemistry · 2010Article
- The highly efficient holding function of the mollusc 'catch' muscle is not based on decelerated myosin head cross-bridge cycles.Proceedings. Biological sciences · 2010Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Molluscan smooth muscle can maintain tension over extended periods with little energy expenditure, a process termed catch. Catch is thought to be regulated by phosphorylation of a thick filament protein, twitchin, and involves two phosphorylation sites, D1 and D2, close to the N and C termini, respectively. This study was initiated to investigate the role of the D2 site and its phosphorylation in the catch mechanism. A peptide was constructed containing the D2 site and flanking immunoglobulin (Ig) motifs. It was shown that the dephosphorylated peptide, but not the phosphorylated form, bound to both actin and myosin. The binding site on actin was within the sequence L10 to P29. This region also binds to loop 2 of the myosin head. The dephosphorylated peptide linked myosin and F-actin and formed a trimeric complex. Electron microscopy revealed that twitchin is distributed on the surface of the thick filament with an axial periodicity of 36.25 nm and it is suggested that the D2 site aligns with the myosin heads. It is proposed that the complex formed with the dephosphorylated D2 site of twitchin, F-actin and myosin represents a component of the mechanical linkage in catch.
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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.