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J. Biol. Chem., Vol. 278, Issue 6, 4331-4338, February 7, 2003

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Phosphoinositide 3-Kinase Activation by Ig Controls de Novo Formation of an Antigen-processing Compartment^*

Marie Granboulan^§, Danielle Lankar, Graça Raposo^¶, Christian Bonnerot, and Claire Hivroz

From the  INSERM U520, ^¶ UMR 144, Institut Curie, 26 rue d'Ulm, 75248 Paris Cedex 05, France

Antigens that bind B cell antigen receptor (BCR) are preferentially and rapidly processed for antigen presentation. The BCR is a multimeric complex containing a signaling module composed of Ig and Ig. Signaling pathways implicated in antigen presentation through the BCR are ill defined. Here we demonstrate that phosphoinositide 3-kinase (PI3K) inhibitors preclude antigen presentation induced by BCR or Ig but not Ig. Unraveling the mechanisms responsible for this inhibition, we show that PI3K inhibitors block neither antigen internalization nor degradation. Rather PI3K inhibitors block de novo formation of a multivesicular antigen processing compartment, which is induced by triggering of the BCR or Ig. Strikingly, we found using fluorescent probes binding specifically to PI3K products that BCR and Ig but not Ig induce PI3K activation in endocytic compartments wherein antigen is transported. Altogether, these results strongly suggest that Ig couples the BCR to PI3K activation that is instrumental for de novo formation of the antigen processing compartment and efficient antigen presentation.

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