ArticleBiochimica et biophysica acta2012
Binding of moesin and ezrin to membranes containing phosphatidylinositol (4,5) bisphosphate: a comparative study of the affinity constants and conformational changes.
Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- A biophysical perspective of the regulatory mechanisms of ezrin/radixin/moesin proteins.Biophysical reviews · 2022Review
- Two Sides of the Coin: Ezrin/Radixin/Moesin and Merlin Control Membrane Structure and Contact Inhibition.International journal of molecular sciences · 2019Review
- Functional integrity of the contractile actin cortex is safeguarded by multiple Diaphanous-related formins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Role of Phosphorylation in Moesin Interactions with PIPBiophysical journal · 2018Article
- Phosphoinositide Binding Inhibits Actin Crosslinking and Polymerization by Palladin.Journal of molecular biology · 2016Article
- Coupling changes in cell shape to chromosome segregation.Nature reviews. Molecular cell biology · 2016Review
- Mode of Ezrin-Membrane Interaction as a Function of PIP2 Binding and Pseudophosphorylation.Biophysical journal · 2016Article
- Phosphatidylinositol 4,5-bisphosphate alters the number of attachment sites between ezrin and actin filaments: a colloidal probe study.The Journal of biological chemistry · 2014Article
- FERM domain of moesin desorbs the basic-rich cytoplasmic domain of l-selectin from the anionic membrane surface.Journal of molecular biology · 2013Article
- Model membranes to shed light on the biochemical and physical properties of ezrin/radixin/moesin.Biochimie · 2013Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The plasma membrane-cytoskeleton interface is a dynamic structure participating in a variety of cellular events. Moesin and ezrin, proteins from the ezrin/radixin/moesin (ERM) family, provide a direct linkage between the cytoskeleton and the membrane via their interaction with phosphatidylinositol 4,5-bisphosphate (PIP(2)). PIP(2) binding is considered as a prerequisite step in ERM activation. The main objective of this work was to compare moesin and ezrin interaction with PIP(2)-containing membranes in terms of affinity and to analyze secondary structure modifications leading eventually to ERM activation. For this purpose, we used two types of biomimetic model membranes, large and giant unilamellar vesicles. The dissociation constant between moesin and PIP(2)-containing large unilamellar vesicles or PIP(2)-containing giant unilamellar vesicles was found to be very similar to that between ezrin and PIP(2)-containing large unilamellar vesicles or PIP(2)-containing giant unilamellar vesicles. In addition, both proteins were found to undergo conformational changes after binding to PIP(2)-containing large unilamellar vesicles. Changes were evidenced by an increased sensitivity to proteolysis, modifications in the fluorescence intensity of the probe attached to the C-terminus and in the proportion of secondary structure elements.
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