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A more recent version of this article appeared on October 27, 2000
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Papers In Press, published online ahead of print August 15, 2000
J. Biol. Chem, 10.1074/jbc.M006725200
Submitted on July 27, 2000
Revised on August 10, 2000
Accepted on August 10, 2000

Phg1p: A Nine-Transmembrane Protein Superfamily MemberInvolved in Dictyostelium Adhesion and Phagocytosis

Sophie Cornillon, Emmanuel Pech, Mohammed Benghezal, Kissia Ravanel, Erin Gaynor, Francois Letourneur, Franz Brückert, and Pierre Cosson

Morphologie, Centre Medical Universitaire, Geneva 4, Ge CH-1211

Corresponding Author: Pierre.Cosson{at}medecine.unige.ch

To identify the molecular mechanisms involved in phagocytosis, we generated random insertion mutants of Dictyostelium discoideum and selected two mutants defective for phagocytosis. Both represented insertions in the same gene, named PHG1. This gene encodes a polytopic membrane protein with an N-terminal lumenal domain and nine potential transmembrane segments. Homologous genes can be identified in many species, however their function is yet to be elucidated. Disruption of PHG1 caused a selective defect in phagocytosis of latex beads and E. coli, but not K. aerogenes bacteria. This defect in phagocytosis was caused by a decrease in the adhesion of mutant cells to phagocytosed particles. These results indicate that the Phg1 protein is involved in the adhesion of Dictyostelium to various substrates, a crucial event of phagocytosis and demonstrate the usefulness of a genetic approach to dissect the molecular events involved in the phagocytic process.


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