ArticleProceedings of the National Academy of Sciences of the United States of America1998
Phosphorylation of a twitchin-related protein controls catch and calcium sensitivity of force production in invertebrate smooth muscle.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 92 citations in OpenAlex.
- The unique biology of catch muscles: insights into structure, function, and robotics innovations.Frontiers in bioengineering and biotechnology · 2025Review
- Evolution, Expression Patterns, and Distribution of Novel Ribbon Worm Predatory and Defensive Toxins.Molecular biology and evolution · 2022Article
- Passive force enhancement in striated muscle.Journal of applied physiology (Bethesda, Md. : 1985) · 2019Review
- Why are muscles strong, and why do they require little energy in eccentric action?Journal of sport and health science · 2018Article
- Article
- Regulation of Contraction by the Thick Filaments in Skeletal Muscle.Biophysical journal · 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
- Large isoforms of UNC-89 (obscurin) are required for muscle cell architecture and optimal calcium release in Caenorhabditis elegans.PloS one · 2012Article
- A force-activated kinase in a catch smooth muscle.Journal of muscle research and cell motility · 2011Article
- The N-terminal region of twitchin binds thick and thin contractile filaments: redundant mechanisms of catch force maintenance.The Journal of biological chemistry · 2010Article
- Mechanism of catch force: tethering of thick and thin filaments by twitchin.Journal of biomedicine & biotechnology · 2010Article
- Twitchin of mollusc smooth muscles can induce "catch"-like properties in human skeletal muscle: support for the assumption that the "catch" state involves twitchin linkages between myofilaments.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2009Article
- Differential distribution of cAMP-dependent protein kinase isoforms in the mantle of the bivalve mollusc Mytilus galloprovincialis.Journal of molecular histology · 2009Article
- Myosin loop 2 is involved in the formation of a trimeric complex of twitchin, actin, and myosin.The Journal of biological chemistry · 2009Article
- Gene expression analyses of essential catch factors in the smooth and striated adductor muscles of larval, juvenile and adult great scallop (Pecten maximus).Journal of muscle research and cell motility · 2009Article
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- Single-molecule force spectroscopy reveals a stepwise unfolding of Caenorhabditis elegans giant protein kinase domains.Biophysical journal · 2008Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
"Catch" is a condition of prolonged, high-force maintenance at resting intracellular Ca2+ concentration ([Ca2+]) and very low energy usage, occurring in invertebrate smooth muscles, including the anterior byssus retractor muscle (ABRM) of Mytilus edulis. Relaxation from catch is rapid on serotonergic nerve stimulation in intact muscles and application of cAMP in permeabilized muscles. This release of catch occurs by protein kinase A-mediated phosphorylation of a high (approximately 600 kDa) molecular mass protein, the regulator of catch. Here, we identify the catch-regulating protein as a homologue of the mini-titin, twitchin, based on (i) a partial cDNA of the purified isolated protein showing 77% amino acid sequence identity to the kinase domain of Aplysia californica twitchin; (ii) a polyclonal antibody to a synthetic peptide in this sequence reacting with the phosphorylated catch-regulating protein band from permeabilized ABRM; and (iii) the similarity of the amino acid composition and molecular weight of the protein to twitchin. In permeabilized ABRM, at all but maximum [Ca2+], phosphorylation of twitchin results in a decreased calcium sensitivity of force production (half-maximum at 2.5 vs. 1.3 microM calcium). At a given submaximal force, with equal numbers of force generators, twitchin phosphorylation increased unloaded shortening velocity approximately 2-fold. These data suggest that aspects of the catch state exist not only at resting [Ca2+], but also at higher submaximal [Ca2+]. The mechanism that gives rise to force maintenance in catch probably operates together, to some extent, with that of cycling myosin crossbridges.
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