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An adhesion molecule in free‐living Dictyostelium amoebae with integrin β features
Author(s) -
Cornillon Sophie,
Gebbie Leigh,
Benghezal Mohammed,
Nair Prashant,
Keller Sebastien,
WehrleHaller Bernhard,
Charette Steve J,
Brückert Franz,
Letourneur François,
Cosson Pierre
Publication year - 2006
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400701
Subject(s) - microbiology and biotechnology , integrin , dictyostelium , cell adhesion , dictyostelium discoideum , cell adhesion molecule , transmembrane protein , adhesion , nectin , biology , cytosol , actin cytoskeleton , cytoskeleton , chemistry , cell , biochemistry , receptor , gene , organic chemistry , enzyme
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 β 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 β chains. This study sheds light on the molecular mechanisms controlling cell adhesion and their establishment during evolution.