Differential roles of PtdIns(4,5)P2 and phosphorylation in moesin activation during Drosophila development. 2010

Fernando Roch, and Cédric Polesello, and Chantal Roubinet, and Marianne Martin, and Christian Roy, and Philippe Valenti, and Sébastien Carreno, and Paul Mangeat, and François Payre
Université de Toulouse UPS, Centre de Biologie du Développement, Toulouse, France. roch@cict.fr

The ezrin, radixin and moesin (ERM) proteins regulate cell membrane architecture in several cellular contexts. Current models propose that ERM activation requires a PtdIns(4,5)P(2)-induced conformational change, followed by phosphorylation of a conserved threonine. However, how these inputs contribute in vivo to orchestrate ERM activation is poorly understood. We addressed this issue by evaluating the contribution of PtdIns(4,5)P(2) and phosphorylation to the regulation of moesin during Drosophila development. Unexpectedly, we found that a form of moesin that cannot be phosphorylated displayed significant activity and could substitute for the endogenous product during wing morphogenesis. By contrast, we also show that PtdIns(4,5)P(2) binding is essential for moesin recruitment to the membrane and for its subsequent phosphorylation. Our data indicate that PtdIns(4,5)P(2) acts as a dosing mechanism that locally regulates ERM membrane recruitment and activation, whereas cycles of phosphorylation and dephosphorylation further control their activity once they have reached the cell cortex.

UI MeSH Term Description Entries
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D008840 Microfilament Proteins Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell. Actin Binding Protein,Actin-Binding Protein,Actin-Binding Proteins,Microfilament Protein,Actin Binding Proteins,Binding Protein, Actin,Protein, Actin Binding,Protein, Actin-Binding,Protein, Microfilament,Proteins, Actin-Binding,Proteins, Microfilament
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D003598 Cytoskeletal Proteins Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible. Proteins, Cytoskeletal
D004330 Drosophila A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology. Fruit Fly, Drosophila,Drosophila Fruit Flies,Drosophila Fruit Fly,Drosophilas,Flies, Drosophila Fruit,Fly, Drosophila Fruit,Fruit Flies, Drosophila
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

Fernando Roch, and Cédric Polesello, and Chantal Roubinet, and Marianne Martin, and Christian Roy, and Philippe Valenti, and Sébastien Carreno, and Paul Mangeat, and François Payre
November 2015, Journal of cell science,
Fernando Roch, and Cédric Polesello, and Chantal Roubinet, and Marianne Martin, and Christian Roy, and Philippe Valenti, and Sébastien Carreno, and Paul Mangeat, and François Payre
January 2018, Journal of cell science,
Fernando Roch, and Cédric Polesello, and Chantal Roubinet, and Marianne Martin, and Christian Roy, and Philippe Valenti, and Sébastien Carreno, and Paul Mangeat, and François Payre
September 2015, Journal of cell science,
Fernando Roch, and Cédric Polesello, and Chantal Roubinet, and Marianne Martin, and Christian Roy, and Philippe Valenti, and Sébastien Carreno, and Paul Mangeat, and François Payre
June 2008, Journal of cell science,
Fernando Roch, and Cédric Polesello, and Chantal Roubinet, and Marianne Martin, and Christian Roy, and Philippe Valenti, and Sébastien Carreno, and Paul Mangeat, and François Payre
October 2012, Journal of chemical biology,
Fernando Roch, and Cédric Polesello, and Chantal Roubinet, and Marianne Martin, and Christian Roy, and Philippe Valenti, and Sébastien Carreno, and Paul Mangeat, and François Payre
August 2005, Current biology : CB,
Fernando Roch, and Cédric Polesello, and Chantal Roubinet, and Marianne Martin, and Christian Roy, and Philippe Valenti, and Sébastien Carreno, and Paul Mangeat, and François Payre
April 2011, The EMBO journal,
Fernando Roch, and Cédric Polesello, and Chantal Roubinet, and Marianne Martin, and Christian Roy, and Philippe Valenti, and Sébastien Carreno, and Paul Mangeat, and François Payre
January 2009, Journal of cell science,
Fernando Roch, and Cédric Polesello, and Chantal Roubinet, and Marianne Martin, and Christian Roy, and Philippe Valenti, and Sébastien Carreno, and Paul Mangeat, and François Payre
February 2010, Current biology : CB,
Fernando Roch, and Cédric Polesello, and Chantal Roubinet, and Marianne Martin, and Christian Roy, and Philippe Valenti, and Sébastien Carreno, and Paul Mangeat, and François Payre
July 1999, Nature cell biology,
Copied contents to your clipboard!