| Literature DB >> 10956646 |
Y Wu1, 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.
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.Entities:
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Year: 2000 PMID： 10956646 DOI： 10.1074/jbc.M005224200
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157