ArticlePlant physiology1999
Inhibitory regulation of higher-plant myosin by Ca2+ ions
Article in Plant physiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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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
36 citing papers in PubMed, 113 citations in OpenAlex.
- The calmodulin-like proteins, CML13 and CML14 function as myosin light chains for the class XI myosins in Arabidopsis.Plant & cell physiology · 2026Article
- Functional characterization of calmodulin-like proteins, CML13 and CML14, as novel light chains of Arabidopsis class VIII myosins.Journal of experimental botany · 2024Article
- Identification of myosin genes and their expression in response to biotic (PVY, PVX, PVS, and PVA) and abiotic (Drought, Heat, Cold, and High-light) stress conditions in potato.Molecular biology reports · 2022Article
- Let's shape again: the concerted molecular action that builds the pollen tube.Plant reproduction · 2022Review
- Quantitative cell biology of tip growth in moss.Plant molecular biology · 2021Review
- Actin Cytoskeleton as Actor in Upstream and Downstream of Calcium Signaling in Plant Cells.International journal of molecular sciences · 2019Review
- Functional Diversity of Class XI Myosins in Arabidopsis thaliana.Plant & cell physiology · 2018Article
- Egg activation-triggered shape change in the Dictyota dichotoma (Phaeophyceae) zygote is actin-myosin and secretion dependent.Annals of botany · 2017Article
- Signaling with Ions: The Keystone for Apical Cell Growth and Morphogenesis in Pollen Tubes.Plant physiology · 2017Review
- The Cytoskeleton and Its Regulation by Calcium and Protons.Plant physiology · 2016Review
- Class XI Myosins Move Specific Organelles in Pollen Tubes and Are Required for Normal Fertility and Pollen Tube Growth in Arabidopsis.Plant physiology · 2015Article
- Navigating the plant cell: intracellular transport logistics in the green kingdom.Molecular biology of the cell · 2015Article
- Interaction between Calcium and Actin in Guard Cell and Pollen Signaling Networks.Plants (Basel, Switzerland) · 2013Review
- Calcium-induced mechanical change in the neck domain alters the activity of plant myosin XI.The Journal of biological chemistry · 2012Article
- Characteristics of light chains of Chara myosin revealed by immunological investigation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2012Article
- Plant-Specific Myosin XI, a Molecular Perspective.Frontiers in plant science · 2012Article
- Microtubule motors and pollen tube growth--still an open question.Protoplasma · 2010Review
- Cytoplasmic streaming enables the distribution of molecules and vesicles in large plant cells.Protoplasma · 2010Review
- Head-neck domain of Arabidopsis myosin XI, MYA2, fused with GFP produces F-actin patterns that coincide with fast organelle streaming in different plant cells.BMC plant biology · 2008Article
- The sliding theory of cytoplasmic streaming: fifty years of progress.Journal of plant research · 2007Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin isolated from the pollen tubes of lily (Lilium longiflorum) is composed of a 170-kD heavy chain (E. Yokota and T. Shimmen [1994] Protoplasma 177: 153-162). Both the motile activity in vitro and the F-actin-stimulated ATPase activity of this myosin were inhibited by Ca2+ at concentrations higher than 10(-6) M. In the Ca2+ range between 10(-6) and 10(-5) M, inhibition of the motile activity was reversible. In contrast, inhibition by more than 10(-5) M Ca2+ was not reversible upon Ca2+ removal. An 18-kD polypeptide that showed the same mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis as that of spinach calmodulin (CaM) was present in this myosin fraction. This polypeptide showed a mobility shift in sodium dodecyl sulfate-polyacrylamide gel electrophoresis in a Ca2+-dependent manner. Furthermore, this polypeptide was recognized by antiserum against spinach CaM. By immunoprecipitation using antiserum against the 170-kD heavy chain, the 18-kD polypeptide was coprecipitated with the 170-kD heavy chain, provided that the Ca2+ concentration was low, indicating that this 18-kD polypeptide is bound to the 170-kD myosin heavy chain. However, the 18-kD polypeptide was dissociated from the 170-kD heavy chain at high Ca2+ concentrations, which irreversibly inhibited the motile activity of this myosin. From these results, it is suggested that the 18-kD polypeptide, which is likely to be CaM, is associated with the 170-kD heavy chain as a light chain. It is also suggested that this polypeptide is involved in the regulation of this myosin by Ca2+. This is the first biochemical basis, to our knowledge, for Ca2+ regulation of cytoplasmic streaming in higher plants.
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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.