Functional identification of a novel 14-3-3 epsilon splicing variant suggests dimerization is not necessary for 14-3-3 epsilon to inhibit UV-induced apoptosis
Functional identification of a novel 14-3-3 epsilon splicing variant suggests dimerization is not necessary for 14-3-3 epsilon to inhibit UV-induced apoptosis
复制标题
新型 14-3-3 epsilon 剪接变体的功能鉴定表明,二聚化对于 14-3-3 epsilon 抑制紫外线诱导的细胞凋亡来说不是必需的
DOI:
10.1016/j.bbrc.2010.04.104
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发表时间:
2010-05-28
影响因子:
3.1
通讯作者:
Yu, Long
中科院分区:
文献类型:
--
作者:
Han, Dingding;Ye, Guangming;Yu, Long
14-3-3 proteins function as a dimer and have been identified to involve in diverse signaling pathways. Here we reported the identification of a novel splicing variant of human 14-3-3 epsilon (14-3-3 epsilon sv), which is derived from a novel exon 1' insertion. The insertion contains a stop codon and leads to a truncated splicing variant of 14-3-3 epsilon. The splicing variant is translated from the exon 2 and results in the deletion of an N-terminal alpha-helix which is crucial for the dimerization. Therefore, the 14-3-3 epsilon sv could not form a dimer with 14-3-3 zeta. However, after UV irradiation 14-3-3 epsilon sv could also support cell survival, suggesting monomer of 14-3-3 epsilon is sufficient to protect cell from apoptosis. (C) 2010 Elsevier Inc. All rights reserved.