TACI (Aglyco-Fc-Fusion)

TACI is a lymphocyte-specific member of the tumor necrosis factor receptor (TNFR) superfamily. It was originally discovered because of its ability to interact with calcium-modulator and cyclophilin ligand (CAML).

Interacting protein(s): BAFF (P7003M), APRIL (P7002F)
Related products: TNF-Receptor Superfamily

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Quick Specs

Description

TACI is a lymphocyte-specific member of the tumor necrosis factor receptor (TNFR) superfamily. It was originally discovered because of its ability to interact with calcium-modulator and cyclophilin ligand (CAML). TACI was later found to play a crucial role in humoral immunity by interacting with two members of the TNF superfamily: BAFF and APRIL. These proteins signal through TACI inducing activation of several transcription factors including NFAT, AP-1, and NF-kappa-B which then modulate cellular activities.

Defects in the function of TACI can lead to immune disorders. Defects in TNFRSF13B are the cause of immunodeficiency common variable type 2 (CVID2). CVID2 is a primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen. The defect results from a failure of B-cell differentiation and impaired secretion of immunoglobulins; the numbers of circulating B-cells is usually in the normal range, but can be low.

In vitro analysis revealed that some individuals with IGAD have impaired isotype class switching to IgA and others may have a post-switch defect. Some individuals initially present with IGAD1 and then develop CVID suggesting that at least in some cases, IGAD and CVID may have a common etiology.

Amino Acid Sequence.

References

1. NF-AT activation induced by a CAML-interacting member of the tumor necrosis factor receptor superfamily. von Buelow G.-U., Bram R.J. Science 278:138-141 (1997)
2. APRIL and TALL-I and receptors BCMA and TACI: system for regulating humoral immunity. Yu G., Boone T., Delaney J., Hawkins N., Kelley M.J., Ramakrishnan M., McCabe S., Qiu W.R., Kornuc M., Xia X.-Z., Guo J., Stolina M., Boyle W.J., Sarosi I., Hsu H., Senaldi G., Theill L.E. Nat. Immunol. 1:252-256 (2000)
3. Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding. Hymowitz S.G., Patel D.R., Wallweber H.J., Runyon S., Yan M., Yin J., Shriver S.K., Gordon N.C., Pan B., Skelton N.J., Kelley R.F., Starovasnik M.A. J. Biol. Chem. 280:7218-7227 (2005)
4. TACI is mutant in common variable immunodeficiency and IgA deficiency. Castigli E., Wilson S.A., Garibyan L., Rachid R., Bonilla F., Schneider L., Geha R.S. Nat. Genet. 37:829-834 (2005)