An adhesion molecule in free-living Dictyostelium amoebae with integrin beta features.
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.
Cornillon
Sophie
S
Département de Physiologie Cellulaire et Métabolisme, Centre Médical Universitaire, 1 rue Michel Servet, 1211 Geneva 4, Switzerland.
Gebbie
Leigh
L
Benghezal
Mohammed
M
Nair
Prashant
P
Keller
Sebastien
S
Wehrle-Haller
Bernhard
B
Charette
Steve J
SJ
Brückert
Franz
F
Letourneur
François
F
Cosson
Pierre
P
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002465:Cell Movement; D017124:Conserved Sequence; D003600:Cytosol / Q000378:metabolism; D004023:Dictyostelium / Q000235:genetics; D017125:Genes, Protozoan; D005982:Glutathione Transferase / Q000378:metabolism; D016023:Integrins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D021382:Protein Sorting Signals; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D011995:Recombination, Genetic; D016608:Talin / Q000378:metabolism
D015815:Cell Adhesion Molecules; D016023:Integrins; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D016608:Talin; D005982:Glutathione Transferase