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A more recent version of this article appeared on July 1, 2003
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Submitted on November 12, 2002
Revised on March 25, 2003
Accepted on April 29, 2003
1 Université de Genève, Centre Médical Universitaire, Département de Morphologie, 1 rue Michel Servet, CH-1211 Genève 4, Switzerland
2 Laboratoire de Biochimie et Biophysique des Systèmes Intégrés, UMR314, CNRS, CEA, Grenoble, France
3 Institut de Biologie et de Chimie des Protéines, UMR 5086 CNRS, Université Lyon I, 7 passage du Vercors, 69367 Lyon Cedex 07, France
* Corresponding author. E-mail address: Mohammed.Benghezal{at}medecine.unige.ch.
The transmembrane 9 (TM9) family of proteins contains numerous members in eukaryotes. Although their function remains essentially unknown in higher eukaryotes, the Dictyostelium discoideum Phg1a TM9 protein was recently reported to be essential for cellular adhesion and phagocytosis.
Here the function of Phg1a and of a new divergent member of the TM9 family called Phg1b was further investigated in Dictyostelium discoideum. The phenotypes of PHG1a, PHG1b and PHG1a/PHG1b double knockout cells revealed that Phg1a and Phg1b proteins play a synergistic but not redundant role in cellular adhesion, phagocytosis, growth and development. Complementation analysis supports a synergistic regulatory function rather than a receptor role for Phg1a and Phg1b proteins. Altogether these results suggest that Phg1 proteins act as regulators of cellular adhesion, possibly by controlling the intracellular transport in the endocytic pathway and the composition of the cell surface.
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