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 Blood, 1 February 2005, Vol. 105, No. 3, pp. 1106-1113.
Prepublished online as a Blood First Edition Paper on September 2, 2004; DOI 10.1182/blood-2003-08-2965.

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IMMUNOBIOLOGY

The adaptor protein 3BP2 associates with VAV guanine nucleotide exchange factors to regulate NFAT activation by the B-cell antigen receptor

Isabelle Foucault, Séverine Le Bras, Céline Charvet, Chéol Moon, Amnon Altman, and Marcel Deckert

From the Institut National de la Santé et de la Recherche Médicale Unité 576 (formerly Unité 343), Hôpital de l'Archet, Nice, France; and the Division of Cell Biology, La Jolla Institute for Allergy and Immunology, San Diego, CA.

Engagement of the B-cell antigen receptor (BCR) activates kinases of the Src and Syk families and signaling complexes assembled by adaptor proteins, which dictate B-cell fate and function. The adaptor 3BP2/SH3BP2, an Abl Src homology domain 3 (SH3)–binding and Syk-kinases interacting protein, exhibits positive regulatory roles in T, natural killer (NK), and basophilic cells. However, its involvement in BCR signaling is completely unknown. Here we show that 3BP2 is tyrosine phosphorylated following BCR aggregation on B lymphoma cells, and that 3BP2 is a substrate for Syk and Fyn, but not Btk. To further explore the function of 3BP2 in B cells, we screened a yeast 2-hybrid B-lymphocyte library and found 3BP2 as a binding partner of Vav proteins. The interaction between 3BP2 and Vav proteins involved both constitutive and inducible mechanisms. 3BP2 also interacted with other components of the BCR signaling pathway, including Syk and phospholipase C {gamma} (PLC-{gamma}). Furthermore, overexpression and RNAi blocking experiments showed that 3BP2 regulated BCR-mediated activation of nuclear factor of activated T cells (NFATs). Finally, evidence was provided that 3BP2 functionally cooperates with Vav proteins and Rho GTPases to activate NFATs. Our results show that 3BP2 may regulate BCR-mediated gene activation through Vav proteins.


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