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

J Biol Chem. 2000 Nov 10;275(45):35478-85. doi: 10.1074/jbc.M005224200.

Y Wu ¹, D Bressette, J A Carrell, T Kaufman, P Feng, K Taylor, Y Gan, Y H Cho, A D Garcia, E Gollatz, D Dimke, D LaFleur, T S Migone, B Nardelli, P Wei, S M Ruben, S J Ullrich, H S Olsen, P Kanakaraj, P A Moore, K P Baker

Affiliations

Affiliation

1 Department of Molecular Biology, Human Genome Sciences, Inc., Rockville, Maryland 20850, USA.

PMID: 10956646 DOI: 10.1074/jbc.M005224200

Abstract

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.

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