Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1932227 | Biochemical and Biophysical Research Communications | 2010 | 6 Pages |
Abstract
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 α-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.
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Biochemistry
Authors
Dingding Han, Guangming Ye, Tingting Liu, Cong Chen, Xianmei Yang, Bo Wan, Yuanwang Pan, Long Yu,