ArticleThe Journal of cell biology1997
Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 74 citations in OpenAlex.
- Double-headed binding of myosin II to F-actin shows the effect of strain on head structure.Journal of structural biology · 2023Article
- Class I Myosins, molecular motors involved in cell migration and cancer.Cell adhesion & migration · 2022Article
- iASPP contributes to cell cortex rigidity, mitotic cell rounding, and spindle positioning.The Journal of cell biology · 2021Article
- A cryo-tomography-based volumetric model of the actin core of mouse vestibular hair cell stereocilia lacking plastin 1.Journal of structural biology · 2020Article
- Human myosin 1e tail but not motor domain replaces fission yeast Myo1 domains to support myosin-I function during endocytosis.Experimental cell research · 2019Article
- Kinetic adaptation of human Myo19 for active mitochondrial transport to growing filopodia tips.Scientific reports · 2017Article
- Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling.Nature structural & molecular biology · 2015Article
- Flexibility within the heads of muscle myosin-2 molecules.Journal of molecular biology · 2014Article
- A vertebrate myosin-I structure reveals unique insights into myosin mechanochemical tuning.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Motor and tail homology 1 (Th1) domains antagonistically control myosin-1 dynamics.Biophysical journal · 2014Article
- Stiffness, working stroke, and force of single-myosin molecules in skeletal muscle: elucidation of these mechanical properties via nonlinear elasticity evaluation.Cellular and molecular life sciences : CMLS · 2013Review
- Regulation and control of myosin-I by the motor and light chain-binding domains.Trends in cell biology · 2013Review
- Localization of myosin 1b to actin protrusions requires phosphoinositide binding.The Journal of biological chemistry · 2010Article
- Leveraging the membrane - cytoskeleton interface with myosin-1.Trends in cell biology · 2010Review
- Molecular model of the microvillar cytoskeleton and organization of the brush border.PloS one · 2010Article
- Control of myosin-I force sensing by alternative splicing.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Removal of the cardiac myosin regulatory light chain increases isometric force production.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009Article
- Diversity of structural behavior in vertebrate conventional myosins complexed with actin.Journal of molecular biology · 2007Article
- The stroke size of myosins: a reevaluation.Journal of muscle research and cell motility · 2006Review
- Association of the leukocyte plasma membrane with the actin cytoskeleton through coiled coil-mediated trimeric coronin 1 molecules.Molecular biology of the cell · 2005Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Brush border myosin-I (BBM-I) is a single-headed myosin found in the microvilli of intestinal epithelial cells, where it forms lateral bridges connecting the core bundle of actin filaments to the plasma membrane. Extending previous observations (Jontes, J.D., E.M. Wilson-Kubalek, and R.A. Milligan. 1995. Nature [Lond.]. 378:751-753), we have used cryoelectron microscopy and helical image analysis to generate three-dimensional (3D) maps of actin filaments decorated with BBM-I in both the presence and absence of 1 mM MgADP. In the improved 3D maps, we are able to see the entire light chain-binding domain, containing density for all three calmodulin light chains. This has enabled us to model a high resolution structure of BBM-I using the crystal structures of the chicken skeletal muscle myosin catalytic domain and essential light chain. Thus, we are able to directly measure the full magnitude of the ADP-dependent tail swing. The approximately 31 degrees swing corresponds to approximately 63 A at the end of the rigid light chain-binding domain. Comparison of the behavior of BBM-I with skeletal and smooth muscle subfragments-1 suggests that there are substantial differences in the structure and energetics of the biochemical transitions in the actomyosin ATPase cycle.
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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.