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Grenoble INP
Synthèse et propriétés de monocristaux, de poudres, films minces ou hétérostructures

Etudes à l'interface avec la matière biologique

Publication de Quentin Lubart 2017

Publié le 23 janvier 2018
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Communiqué du 30 décembre 2017 au 31 décembre 2017

Le papier "Role of Phosphorylation in Moesin Interactions with PIP2-Containing Biomimetic Membranes" a été publié dans Biophysical Journal

moesine.PNG

moesine.PNG

Ici  vous trouverez les papier de  Quentin Lubart

"Moesin, a protein of the ezrin, radixin, and moesin family, which links the plasma membrane to the cytoskeleton, is involved in multiple physiological and pathological processes, including viral budding and infection. Its interaction with the plasma membrane occurs via a key phosphoinositide, the phosphatidyl(4,5)inositol-bisphosphate (PIP2), and phosphorylation of residue T558, which has been shown to contribute, in cellulo, to a conformationally open protein. We study the impact of a double phosphomimetic mutation of moesin (T235D, T558D), which mimics the phosphorylation state of the protein, on protein/PIP2/microtubule interactions. Analytical ultracentrifugation in the micromolar range showed moesin in the monomer and dimer forms, with wild-type (WT) moesin containing a slightly larger fraction (∼30%) of dimers than DD moesin (10–20%). Only DD moesin was responsive to PIP2 in its micellar form. Quantitative cosedimentation assays using large unilamellar vesicles and quartz crystal microbalance on supported lipid bilayers containing PIP2 reveal a specific cooperative interaction for DD moesin with an ability to bind two PIP2 molecules simultaneously, whereas WT moesin was able to bind only one. In addition, DD moesin could subsequently interact with microtubules, whereas WT moesin was unable to do so. Altogether, our results point to an important role of these two phosphorylation sites in the opening of moesin: since DD moesin is intrinsically in a more open conformation than WT moesin, this intermolecular interaction is reinforced by its binding to PIP2. We also highlight important differences between moesin and ezrin, which appear to be finely regulated and to exhibit distinct molecular behaviors."



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Rédigé par Maria Carmen Jimenez Arevalo

mise à jour le 23 janvier 2018

  • Tutelle CNRS
  • Tutelle Grenoble INP
Communauté Université Grenoble Alpes