Active site trapping of nucleotide by smooth and non-muscle myosins
Abstract
The folded 10 S monomer conformation of smooth muscle myosin traps the hydrolysis products ADP and Pi in its active sites. To test the significance of this, we have searched for equivalent trapping in other conformational and assembly states of avian gizzard and brush border myosins, using formycin triphosphate (FTP) as an ATP analogue. When myosin monomers were in the straight-tail 6 S conformation, the hydrolysis products were released at about 0.03 s-1. Adoption of the folded 10 S monomer conformation reduced this rate by more than 100-fold, effectively trapping the products FDP and Pi in the active sites. This profound inhibition of product release occurred only on formation of the looped tail monomer conformation. In vitro-assembled myosin filaments released products at a comparable rate to free straight-tail 6 S monomers, and smooth muscle heavy meromyosin, which lacks the C-terminal two-thirds of the myosin tail, also did not trap the products in this way. Phosphorylation of the myosin regulatory light chain had no effect on the rate of product release from straight-tail 6 S myosin monomers or from myosin filaments. Rather, it allowed actin to accelerate product release. Phosphorylation acted also to destabilize the folded monomer conformation, causing the recruitment of molecules from the pool of folded monomers into the myosin filaments. The two processes of contraction and filament assembly are thus both controlled in vitro by light-chain phosphorylation. A similar linked control in vivo would allow the organization of myosin in the cell to adapt itself continuously to the pattern of contractile activity.
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Many myosins are inhibited for actin interaction in a light chain-dependent manner by sequences downstream of their motor domains.
“Many myosins are inhibited for actin interaction in a light chain-dependent manner by sequences downstream of their motor domains (Cross et al., 1988; Mooseker and Cheney, 1995).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Cross et al., 1988
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- Authors
- Cross, R. A., Jackson, A. P., Citi, S., Kendrick-Jones, J., & Bagshaw, C. R.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- University of Leicester (GB)
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1988-09
- Volume
- 203
- Issue
- 1
- Pages
- 173-181
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2013462701
- Cited by
- 105
- References
- 31
- Citations by year
- 2026: 6 · 2025: 2 · 2024: 3 · 2023: 5 · 2022: 4 · 2021: 3 · 2020: 3 · 2019: 2 · 2018: 2 · 2017: 1 · 2016: 5 · 2014: 2 · 2013: 1 · 2012: 3
- FWCI
- 3.93
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- smooth muscle myosin, myosin filament assembly, heavy meromyosin, ADP release, inorganic phosphate release, regulatory light chain phosphorylation, actin
- MeSH terms
- Adenosine Triphosphate, Animals, Binding Sites, Chickens, Formycins, Microvilli, Muscle, Smooth, Myosins, Phosphorylation, Protein Conformation, Ribonucleotides, Myosin Subfragments
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