Assembly and regulation of the CD40 receptor complex in human B cells.
Assembly and regulation of the CD40 receptor complex in human B cells.
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人类B细胞中CD40受体复合物的组装和调节。
DOI：
10.1084/jem.186.2.337
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发表时间：
1997-07-21
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CD40是肿瘤坏死因子受体超家族的成员。对人B细胞的研究表明，CD154(gp39，CD40L)与CD40结合后，可使肿瘤坏死因子受体相关因子2(TRAF2)和TRAF3与受体复合体结合，下调细胞内非受体相关TRAF的表达，增加细胞表面Fas的表达。通过白介素4受体和CD40的联合信号诱导Fas的表达增加，同时TRAF2的水平也相应增加，但不包括TRAF3，后者被招募到受体复合体中。相反，膜免疫球蛋白和CD40的结合限制了Fas的上调，并减少了TRAF2相对于TRAF3对CD40受体复合体的募集。这些研究表明，CD40受体复合体的TRAF组成可以被影响B细胞分化的信号改变。
CD40 is a member of the tumor necrosis factor (TNF) receptor superfamily. Studies with human B cells show that the binding of CD154 (gp39, CD40L) to CD40 recruits TNF receptor– associated factor 2 (TRAF2) and TRAF3 to the receptor complex, induces the downregulation of the nonreceptor-associated TRAFs in the cell and induces an increased expression of Fas on the cell surface. Combined signaling through the interluekin 4 receptor and CD40 induces an increased expression of Fas with a commensurate increase in the level of TRAF2, but not TRAF3, that is recruited to the receptor complex. In contrast, engagement of the membrane immunoglobulin and CD40 limits Fas upregulation and reduces the recruitment of TRAF2, relative to TRAF3, to the CD40 receptor complex. These studies show that the TRAF composition of the CD40 receptor complex can be altered by signals that influence B cell differentiation.