ArticleBiophysical journal2001
The myosin cross-bridge cycle and its control by twitchin phosphorylation in catch muscle.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 37 citations in OpenAlex.
- The unique biology of catch muscles: insights into structure, function, and robotics innovations.Frontiers in bioengineering and biotechnology · 2025Review
- Mechanism and Function of the Catch State in Molluscan Smooth Muscle: A Historical Perspective.International journal of molecular sciences · 2020Review
- 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
- A force-activated kinase in a catch smooth muscle.Journal of muscle research and cell motility · 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
- Mechanism of catch force: tethering of thick and thin filaments by twitchin.Journal of biomedicine & biotechnology · 2010Article
- 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
- Myosin cross-bridge kinetics and the mechanism of catch.Biophysical journal · 2007Article
- Catch force links and the low to high force transition of myosin.Biophysical journal · 2006Article
- No effect of twitchin phosphorylation on the rate of myosin head detachment in molluscan catch muscle: are myosin heads involved in the catch state?Pflugers Archiv : European journal of physiology · 2005Article
- Effects of vanadate, phosphate and 2,3-butanedione monoxime (BDM) on skinned molluscan catch muscle.Pflugers Archiv : European journal of physiology · 2005Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The anterior byssus retractor muscle of Mytilus edulis was used to characterize the myosin cross-bridge during catch, a state of tonic force maintenance with a very low rate of energy utilization. Addition of MgATP to permeabilized muscles in high force rigor at pCa > 8 results in a rapid loss of some force followed by a very slow rate of relaxation that is characteristic of catch. The fast component is slowed 3-4-fold in the presence of 1 mM MgADP, but the distribution between the fast and slow (catch) components is not dependent on [MgADP]. Phosphorylation of twitchin results in loss of the catch component. Fewer than 4% of the myosin heads have ADP bound in rigor, and the time course (0.2-10 s) of ADP formation following release of ATP from caged ATP is similar whether or not twitchin is phosphorylated. This suggests that MgATP binding to the cross-bridge and subsequent splitting are independent of twitchin phosphorylation, but detachment occurs only if twitchin is phosphorylated. A similar dependence of detachment on twitchin phosphorylation is seen with AMP-PNP and ATPgammaS. Single turnover experiments on bound ADP suggest an increase in the rate of release of ADP from the cross-bridge when catch is released by phosphorylation of twitchin. Low [Ca(2+)] and unphosphorylated twitchin appear to cause catch by 1) markedly slowing ADP release from attached cross-bridges and 2) preventing detachment following ATP binding to the rigor cross-bridge.
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