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Vol. 14, Issue 7, 2890-2899, July 2003

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Synergistic Control of Cellular Adhesion by Transmembrane 9 Proteins

Mohammed Benghezal ^* , Sophie Cornillon ^*, Leigh Gebbie ^*, Laeticia Alibaud ^*, Franz Brückert , François Letourneur , and Pierre Cosson ^*

^*Université de Genève, Centre Médical Universitaire, Département de Morphologie, CH-1211 Geneva, Switzerland; Laboratoire de Biochimie et Biophysique des Systèmes Intégrés, Unité Mixte Recherche 314, Centre National de la Recherche Scientifique, CEA, Grenoble, France; and Institut de Biologie et de Chimie des Protéines, Unité Mixte Recherche 5086 Centre National de la Recherche Scientifique, Université Lyon I, 69367 Lyon, France

Submitted November 12, 2002; Revised March 25, 2003; Accepted March 25, 2003
Monitoring Editor: Mark Ginsberg

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. Herein, the function of Phg1a and of a new divergent member of the TM9 family called Phg1b was further investigated in D. 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. Together, 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.

Corresponding author. E-mail address: mohammed.benghezal{at}medecine.unige.ch.

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