ReviewJournal of muscle research and cell motility2005
Twitchin as a regulator of catch contraction in molluscan smooth muscle.
Review in Journal of muscle research and cell motility, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
17 citing papers in PubMed, 44 citations in OpenAlex.
- Prevalence and Mechanisms of Sustained Force Production in the Musculature of the Southern Alligator Lizard (Elgaria multicarinata).Journal of experimental zoology. Part A, Ecological and integrative physiology · 2026Article
- How to Reproduce in the Siberian Winter: Proteome Dynamics Reveals the Timing of Reproduction-Related Processes in an Amphipod Species Endemic to Lake Baikal.Ecology and evolution · 2025Article
- Importance of clitellar tissue in the regeneration ability of earthworm Eudrilus eugeniae.Functional & integrative genomics · 2022Article
- Evolution, Expression Patterns, and Distribution of Novel Ribbon Worm Predatory and Defensive Toxins.Molecular biology and evolution · 2022Article
- Making waves: A proposed new role for myosin-binding protein C in regulating oscillatory contractions in vertebrate striated muscle.The Journal of general physiology · 2021Article
- Calcium-dependent titin-thin filament interactions in muscle: observations and theory.Journal of muscle research and cell motility · 2020Review
- Basic science and clinical use of eccentric contractions: History and uncertainties.Journal of sport and health science · 2018Review
- Nonparametric Model of Smooth Muscle Force Production During Electrical Stimulation.Journal of computational biology : a journal of computational molecular cell biology · 2017Article
- Serotonin modulates muscle function in the medicinal leech Hirudo verbana.Biology letters · 2011Article
- The highly efficient holding function of the mollusc 'catch' muscle is not based on decelerated myosin head cross-bridge cycles.Proceedings. Biological sciences · 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
- Contamination of bivalve haemolymph samples by adductor muscle components: implications for biomarker studies.Ecotoxicology (London, England) · 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
- Article
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- Molecular basis of the catch state in molluscan smooth muscles: a catchy challenge.Journal of muscle research and cell motility · 2008Review
- Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch.The Journal of experimental biology · 2007Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Molluscan catch muscle can maintain tension for a long time with little energy consumption. This unique phenomenon is regulated by phosphorylation and dephosphorylation of twitchin, a member of the titin/connectin family. The catch state is induced by a decrease of intracellular Ca2+ after the active contraction and is terminated by the phosphorylation of twitchin by the cAMP-dependent protein kinase (PKA). Twitchin, from the well-known catch muscle, the anterior byssus retractor muscle (ABRM) of the mollusc Mytilus, incorporates three phosphates into two major sites D1 and D2, and some minor sites. Dephosphorylation is required for re-entering the catch state. Myosin, actin and twitchin are essential players in the mechanism responsible for catch during which force is maintained while myosin cross-bridge cycling is very slow. Dephosphorylation of twitchin allows it to bind to F-actin, whereas phosphorylation decreases the affinity of the two proteins. Twitchin has been also been shown to be a thick filament-binding protein. These findings raise the possibility that twitchin regulates the myosin cross-bridge cycle and force output by interacting with both actin and myosin resulting in a structure that connects thick and thin filaments in a phosphorylation-dependent manner.
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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.