ArticleCell biochemistry and biophysics2013
Differential effects of G- and F-actin on the plasma membrane calcium pump activity.
Article in Cell biochemistry and biophysics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Rules of life at the interface of calcium signaling and mechanobiology.APL bioengineering · 2025Review
- The calcium pump PMCA4b promotes epithelial cell polarization and lumen formation.Communications biology · 2025Article
- Tubulin Regulates Plasma Membrane CaCell biochemistry and biophysics · 2024Review
- Intensive stretch-activated CRT-PMCA1 feedback loop promoted apoptosis of myoblasts through CaApoptosis : an international journal on programmed cell death · 2022Article
- Signaling Enzymes and Ion Channels Being Modulated by the Actin Cytoskeleton at the Plasma Membrane.International journal of molecular sciences · 2021Review
- Article
- Charge-dependent interactions of monomeric and filamentous actin with lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Sphingomyelin-induced inhibition of the plasma membrane calcium ATPase causes neurodegeneration in type A Niemann-Pick disease.Molecular psychiatry · 2017Article
- Cofilin recruits F-actin to SPCA1 and promotes Ca2+-mediated secretory cargo sorting.The Journal of cell biology · 2014Article
- The plasma membrane calcium pump: new ways to look at an old enzyme.The Journal of biological chemistry · 2014Review
- Conformational changes produced by ATP binding to the plasma membrane calcium pump.The Journal of biological chemistry · 2013Article
- Plasma membrane calcium ATPase activity is regulated by actin oligomers through direct interaction.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
We have previously shown that plasma membrane calcium ATPase (PMCA) pump activity is affected by the membrane protein concentration (Vanagas et al., Biochim Biophys Acta 1768:1641-1644, 2007). The results of this study provided evidence for the involvement of the actin cytoskeleton. In this study, we explored the relationship between the polymerization state of actin and its effects on purified PMCA activity. Our results show that PMCA associates with the actin cytoskeleton and this interaction causes a modulation of the catalytic activity involving the phosphorylated intermediate of the pump. The state of actin polymerization determines whether it acts as an activator or an inhibitor of the pump: G-actin and/or short oligomers activate the pump, while F-actin inhibits it. The effects of actin on PMCA are the consequence of direct interaction as demonstrated by immunoblotting and cosedimentation experiments. Taken together, these findings suggest that interactions with actin play a dynamic role in the regulation of PMCA-mediated Ca(2+) extrusion through the membrane. Our results provide further evidence of the activation-inhibition phenomenon as a property of many cytoskeleton-associated membrane proteins where the cytoskeleton is no longer restricted to a mechanical function but is dynamically involved in modulating the activity of integral proteins with which it interacts.
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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.