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An adhesion molecule in free-living Dictyostelium amoebae with integrin beta features |
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Published in | EMBO reports. 2006, vol. 7, no. 6, p. 617-21 | |
Abstract | The study of free-living amoebae has proven valuable to explain the molecular mechanisms controlling phagocytosis, cell adhesion and motility. In this study, we identified a new adhesion molecule in Dictyostelium amoebae. The SibA (Similar to Integrin Beta) protein is a type I transmembrane protein, and its cytosolic, transmembrane and extracellular domains contain features also found in integrin beta chains. In addition, the conserved cytosolic domain of SibA interacts with talin, a well-characterized partner of mammalian integrins. Finally, genetic inactivation of SIBA affects adhesion to phagocytic particles, as well as cell adhesion and spreading on its substrate. It does not visibly alter the organization of the actin cytoskeleton, cellular migration or multicellular development. Our results indicate that the SibA protein is a Dictyostelium cell adhesion molecule presenting structural and functional similarities to metazoan integrin beta chains. This study sheds light on the molecular mechanisms controlling cell adhesion and their establishment during evolution. | |
Keywords | Amino Acid Motifs — Amino Acid Sequence — Animals — Cell Adhesion — Cell Adhesion Molecules/chemistry/genetics/metabolism — Cell Movement — Conserved Sequence — Cytosol/metabolism — Dictyostelium/genetics — Genes — Protozoan — Glutathione Transferase/metabolism — Integrins/chemistry/genetics/metabolism — Molecular Sequence Data — Mutation — Protein Sorting Signals — Protein Structure — Tertiary — Recombinant Fusion Proteins/chemistry/metabolism — Recombination — Genetic — Talin/metabolism | |
Identifiers | PMID: 16699495 | |
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Research groups | Migration cellulaire (645) Phagocytose (140) | |
Citation (ISO format) | CORNILLON, Sophie Marie et al. An adhesion molecule in free-living Dictyostelium amoebae with integrin beta features. In: EMBO reports, 2006, vol. 7, n° 6, p. 617-21. doi: 10.1038/sj.embor.7400701 https://archive-ouverte.unige.ch/unige:26027 |