Integrin-linked Kinase Interactions with ELMO2 Modulate Cell Polarity
| Autor: | Tames Irvine, Lina Dagnino, Gilles A. Lajoie, Kodi S. Ravichandran, Sudhir J.A. D'Souza, Ernest Ho, Gregory J.A. Vilk |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
rho GTP-Binding Proteins
Keratinocytes Male Proteomics Scaffold protein Proteome Medical Physiology Pediatrics GTP Phosphohydrolases Mice Cell Movement Cell polarity Cytoskeleton Cells Cultured Microscopy Cultured Microscopy Confocal biology Adaptor Proteins Cell Polarity Signal transducing adaptor protein Articles Protein-Serine-Threonine Kinases Ankyrin Repeat Cell biology Confocal embryonic structures Lamellipodium Protein Binding Cells Green Fluorescent Proteins Immunoblotting Morphogenesis Medical Biochemistry Protein Serine-Threonine Kinases Animals Humans Immunoprecipitation Integrin-linked kinase Molecular Biology Adaptor Proteins Signal Transducing Binding Sites Signal Transducing Infant Newborn Infant Cell Biology Newborn Cytoskeletal Proteins Animals Newborn biology.protein RhoG |
| Zdroj: | Physiology and Pharmacology Publications |
| ISSN: | 1939-4586 1059-1524 |
| DOI: | 10.1091/mbc.e09-01-0050 |
| Popis: | Cell polarization is a key prerequisite for directed migration during development, tissue regeneration, and metastasis. Integrin-linked kinase (ILK) is a scaffold protein essential for cell polarization, but very little is known about the precise mechanisms whereby ILK modulates polarization in normal epithelia. Elucidating these mechanisms is essential to understand tissue morphogenesis, transformation, and repair. Here we identify a novel ILK protein complex that includes Engulfment and Cell Motility 2 (ELMO2). We also demonstrate the presence of RhoG in ILK–ELMO2 complexes, and the localization of this multiprotein species specifically to the leading lamellipodia of polarized cells. Significantly, the ability of RhoG to bind ELMO is crucial for ILK induction of cell polarization, and the joint expression of ILK and ELMO2 synergistically promotes the induction of front-rear polarity and haptotactic migration. This places RhoG–ELMO2–ILK complexes in a key position for the development of cell polarity and forward movement. Although ILK is a component of many diverse multiprotein species that may contribute to cell polarization, expression of dominant-negative ELMO2 mutants is sufficient to abolish the ability of ILK to promote cell polarization. Thus, its interaction with ELMO2 and RhoG is essential for the ability of ILK to induce front-rear cell polarity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|