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Tumor necrosis factor (TNF) receptor superfamily member TACI is a high affinity receptor for TNF family members APRIL and BLyS.

Wu Y., Bressette D., Carrell J.A., Kaufman T., Feng P., Taylor K., Gan Y., Cho Y.H., Garcia A.D., Gollatz E., Dimke D., LaFleur D., Migone T.S., Nardelli B., Wei P., Ruben S.M., Ullrich S.J., Olsen H.S., Kanakaraj P., Moore P.A., Baker K.P.

An expression cloning approach was employed to identify the receptor for B-lymphocyte stimulator (BLyS) and identified the tumor necrosis factor receptor superfamily member TACI as a BLyS-binding protein. Expression of TACI in HEK293T cells confers on the cells the ability to bind BLyS with subnanomolar affinity. Furthermore, a TACI-Fc fusion protein recognizes both the cleaved, soluble form of BLyS as well as the membrane BLyS present on the cell surface of a recombinant cell line. TACI mRNA is found predominantly in B-cells and correlates with BLyS binding in a panel of B-cell lines. We also demonstrate that TACI interacts with nanomolar affinity with the BLyS-related tumor necrosis factor homologue APRIL for which no clear in vivo role has been described. BLyS and APRIL are capable of signaling through TACI to mediate NF-kappaB responses in HEK293 cells. We conclude that TACI is a receptor for BLyS and APRIL and discuss the implications for B-cell biology.

J. Biol. Chem. 275:35478-35485(2000) [PubMed] [Europe PMC]

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