Phosphorylation of TRAF2 inhibits binding to the CD40 cytoplasmic domain
Phosphorylation of TRAF2 inhibits binding to the CD40 cytoplasmic domain
复制标题
DOI：
10.1006/bbrc.1999.0385
复制
发表时间：
1999-03-24
影响因子：
3.1
通讯作者：
Cherayil, BJ
中科院分区：
文献类型：
--
作者：
Chaudhuri, A;Orme, S;Cherayil, BJ
TRAF 2是一种信号转导衔接子分子，可与CD 40胞质结构域结合。我们已经发现，当在293细胞中瞬时过表达时，它主要在丝氨酸残基上被磷酸化。磷酸化似乎与在这些情况下由TRAF 2激活的信号传导事件有关，因为发现两个非功能性突变体的磷酸化显著低于野生型蛋白。此外，TRAF 2的磷酸化状态对该蛋白结合CD 40的能力具有显著影响，正如我们观察到的CD 40胞质结构域优先与磷酸化不足的TRAF 2相互作用以及磷酸酶处理显著增强TRAF 2与CD 40的结合所证明的。我们从这些研究中得出结论，TRAFB的磷酸化可能通过其影响CD 40-TRAF 2相互作用的能力在调节信号转导中发挥重要作用。(C)北京：科学出版社.
TRAF2 is a signal transducing adaptor molecule which binds to the CD40 cytoplasmic domain. We have found that it is phosphorylated, predominantly on serine residues, when transiently overexpressed in 293 cells. The phosphorylation appears to be related to the signaling events that are activated by TRAF2 under these circumstances, since two nonfunctional mutants were found to be phosphorylated significantly less than the wild-type protein.,Furthermore, the phosphorylation status of TRAF2:had significant effects Oh the ability of the protein to bind to CD40, as evidenced by our observations that the CD40 cytoplasmic domain interacted preferentially with underphosphorylated TRAF2 and that phosphatase treatment significantly enhanced the binding of TRAF2 to CD40. We conclude from these studies that the phosphorylation of TRAFB is likely to play an important role in regulating Signaling by virtue of its ability to influence the CD40-TRAF2 interaction. (C) 1999 Academic Press.