Ezrin regulates microvillus morphogenesis by promoting distinct activities of Eps8 proteins
| Autor: | Marcel M.L. Cunha, Ingrid Zwaenepoel, Alexandra Naba, Laurence Del Maestro, Monique Arpin, Etienne Formstecher, Daniel Louvard |
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| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
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Swine Sus scrofa macromolecular substances Biology environment and public health digestive system EPS8 Kidney Tubules Proximal Ezrin medicine Animals Actin filament polymerization Protein Interaction Domains and Motifs Cytoskeleton Molecular Biology Actin Microvilli digestive oral and skin physiology Intracellular Signaling Peptides and Proteins Microvillus assembly Epithelial Cells Cell Biology Articles Microvillus Actins Cell biology Cytoskeletal Proteins medicine.anatomical_structure LLC-PK1 Cells |
| Zdroj: | Molecular Biology of the Cell |
| ISSN: | 1939-4586 1059-1524 |
| Popis: | The membrane cytoskeleton linker ezrin differentially regulates the activity of Eps8 and Eps8L1a in microvillar actin-F assembly. Eps8L1a displays F-actin capping activity, therefore controlling microvillus length, whereas, as previously shown, Eps8 displays bundling activity. The mechanisms that regulate actin filament polymerization resulting in the morphogenesis of the brush border microvilli in epithelial cells remain unknown. Eps8, the prototype of a family of proteins capable of capping and bundling actin filaments, has been shown to bundle the microvillar actin filaments. We report that Eps8L1a, a member of the Eps8 family and a novel ezrin-interacting partner, controls microvillus length through its capping activity. Depletion of Eps8L1a leads to the formation of long microvilli, whereas its overexpression has the opposite effect. We demonstrate that ezrin differentially modulates the actin-capping and -bundling activities of Eps8 and Eps8L1a during microvillus assembly. Coexpression of ezrin with Eps8 promotes the formation of membrane ruffles and tufts of microvilli, whereas expression of ezrin and Eps8L1a induces the clustering of actin-containing structures at the cell surface. These distinct morphological changes are neither observed when a mutant of ezrin defective in its binding to Eps8/Eps8L1a is coexpressed with Eps8 or Eps8L1a nor observed when ezrin is expressed with mutants of Eps8 or Eps8L1a defective in the actin-bundling or -capping activities, respectively. Our data show a synergistic effect of ezrin and Eps8 proteins in the assembly and organization of actin microvillar filaments. |
| Databáze: | OpenAIRE |
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