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B, Elk-1, c-Jun N-Terminal Kinase, and p38 Mitogen-Activated Protein Kinase1
*
Laboratory of Experimental Endocrinology, Faculty of Medicine, University of Crete, Heraklion, Greece;
Institut National de la Santé et de la Recherche Médicale, Unité 131, Institut Paris-Sud sur les Cytokines, Clamart, France; and
Department of Oncology, Institute of Medical Science, University of Tokyo, Tokyo, Japan
BCMA (B cell maturation) is a nonglycosylated integral membrane
type I protein that is preferentially expressed in mature B
lymphocytes. Previously, we reported in a human malignant myeloma cell
line that BCMA is not primarily present on the cell surface but lies in
a perinuclear structure that partially overlaps the Golgi apparatus. We
now show that in transiently or stably transfected cells, BCMA is
located on the cell surface, as well as in a perinulear Golgi-like
structure. We also show that overexpression of BCMA in 293 cells
activates NF-
B, Elk-1, the c-Jun N-terminal kinase, and the p38
mitogen-activated protein kinase. Coimmunoprecipitation experiments
performed in transfected cells showed that BCMA associates with
TNFR-associated factor (TRAF) 1, TRAF2, and TRAF3 adaptor proteins.
Analysis of deletion mutants of the intracytoplasmic tail of BCMA
showed that the 25-aa protein segment, from position 119 to 143,
conserved between mouse and human BCMA, is essential for its
association with the TRAFs and the activation of NF-B, Elk-1, and
c-Jun N-terminal kinase. BCMA belongs structurally to the TNFR family.
Its unique TNFR motif corresponds to a variant motif present in the
fourth repeat of the TNFRI molecule. This study confirms that BCMA is a
functional member of the TNFR superfamily. Furthermore, as BCMA is
lacking a "death domain" and its overexpression activates NF-B
and c-Jun N-terminal kinase, we can reasonably hypothesize that upon
binding of its corresponding ligand BCMA transduces signals for cell
survival and proliferation.
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