[ David Communi ]
Our major goal is the discovery of novel molecules involved in signal transduction (immune and inflammatory responses, neuronal function and stem cell physiology), i.e. ligands for orphan GPCRs and intracellular second messengers. We also focus on the study of their post-translational modifications (e.g. proteolytic processing, phosphorylation, glycosylation,...). The current research concerns essentially the purification of peptides and proteins by 2D-electrophoresis and multidimensional HPLC, followed by their structural analysis by mass spectrometry (MALDI and nanoLC Q-TOF systems), as well as their functional and physiological characterisation.
David Communi graduated in Chemistry (biochemistry) from the Free University of Brussels in 1990. He obtained his PhD in the group of Profs. Jacques Dumont and Christophe Erneux (Free University of Brussels) in 1995: his work concerned the study of the structure/function relationships of kinases and phosphatases involved in the metabolism of inositol polyphosphates and phosphoinositides. David Communi was then a post-doctoral fellow in the group of Prof. Joel Vandekerckhove (University of Ghent) for one year (1999), to study by mass spectrometry the post-translational modifications and the potential partners of enzymes involved in the metabolism of inositol polyphosphates in astrocytes.
He is presently a staff scientist (Senior Research Associate from the FRS-FNRS) at the IRIBHM (proteomic plateform): he is involved in the structural analysis (chromatographic and gel purification, mass spectrometry) and in the functional characterization of novel ligand/orphan GPCR couples regulating the physiology of immune, brain and stem cells. David Communi teaches protein chemistry and proteomics in biomedical sciences at the Free University of Brussels.
Phone: +32-(0)2-5554150/4221 - Email: firstname.lastname@example.org
Main recent publications
Communi D., Gevaert K., Demol H., Vandekerckhove J. and Erneux
A novel receptor-mediated regulation mechanism of type I inositol polyphosphate 5-phosphatase by calcium:calmodulin-dependent protein kinase II phosphorylation.
J. Biol. Chem. 276: 38738-38747 (2001).
Wittamer V., Franssen J.-D., Vulcano M., Mirjolet J.-F., Le Poul E., Migeotte I., Brézillon S., Tyldesley R., Blanpain C., Detheux M., Mantovani A., Sozzani S., Vassart G., Parmentier M. and Communi D.
Specific recruitment of antigen-presenting cells by chemerin, a novel processed ligand from human inflammatory fluids.
J. Exp. Med. 198: 977-985 (2003).
Migeotte I., Riboldi E., Franssen J.-D., Grégoire F., Loison C., Wittamer V., Detheux M., Robberecht P., Costagliola S., Vassart G., Sozzani S., Parmentier M. and Communi D.
Identification and characterization of an endogenous chemotactic ligand specific for FPRL2.
J. Exp. Med. 201: 83-93 (2005).
Wittamer V., Bondue B., Guillabert A., Vassart G., Parmentier M. and Communi D.
Neutrophil-mediated maturation of chemerin : a link between innate and adaptive immunity.
J. Immunol. 175: 487-493 (2005).