ArticleEMBO reports2002
Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium.
Article in EMBO reports, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed.
- Switch-2 determines MgFrontiers in physiology · 2024Article
- Filamentous tangles with nemaline rods in MYH2 myopathy: a novel phenotype.Acta neuropathologica communications · 2021Article
- Unraveling a Force-Generating Allosteric Pathway of Actomyosin Communication Associated with ADP and PInternational journal of molecular sciences · 2020Article
- Single-molecule analysis reveals that regulatory light chains fine-tune skeletal myosin II function.The Journal of biological chemistry · 2020Article
- Electrostatic interactions in the force-generating region of the human cardiac myosin modulate ADP dissociation from actomyosin.Biochemical and biophysical research communications · 2019Article
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
- The Conserved Lysine-265 Allosterically Modulates Nucleotide- and Actin-binding Site Coupling in Myosin-2.Scientific reports · 2017Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- Mapping interactions between myosin relay and converter domains that power muscle function.The Journal of biological chemistry · 2014Article
- Article
- Reduced atomic pair-interaction design (RAPID) model for simulations of proteins.The Journal of chemical physics · 2013Article
- The mechanism of the converter domain rotation in the recovery stroke of myosin motor protein.Proteins · 2012Article
- Article
- Alternative relay and converter domains tune native muscle myosin isoform function in Drosophila.Journal of molecular biology · 2012Article
- Structure-based predictive models for allosteric hot spots.PLoS computational biology · 2009Article
- Allosteric transitions in biological nanomachines are described by robust normal modes of elastic networks.Current protein & peptide science · 2009Article
- Alternative versions of the myosin relay domain differentially respond to load to influence Drosophila muscle kinetics.Biophysical journal · 2008Article
- Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function.Journal of molecular biology · 2008Article
- Predicting allosteric communication in myosin via a pathway of conserved residues.Journal of molecular biology · 2007Article
- Mechanochemical coupling in the myosin motor domain. II. Analysis of critical residues.PLoS computational biology · 2007Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dominant-negative inhibition is a powerful genetic tool for the characterization of gene function in vivo, based on the specific impairment of a gene product by the coexpression of a mutant version of the same gene product. We describe the detailed characterization of two myosin constructs containing either point mutations F487A or F506G in the relay region. Dictyostelium cells transformed with F487A or F506G myosin are unable to undergo processes that require myosin II function, including fruiting-body formation, normal cytokinesis and growth in suspension. Our results show that the dominant-negative inhibition of myosin function is caused by disruption of the communication between active site and lever arm, which blocks motor activity completely, and perturbation of the communication between active site and actin-binding site, leading to an approximately 100-fold increase in the mutants' affinity for actin in the presence of ATP.
Indexed as
Identifiers
What OpenQuestion holds
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.