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

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...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2010-05, Vol.396 (2), p.401-406
Main Authors: Han, Dingding, Ye, Guangming, Liu, Tingting, Chen, Cong, Yang, Xianmei, Wan, Bo, Pan, Yuanwang, Yu, Long
Format: Article
Language:English
Subjects:
14-3-3 epsilon
14-3-3 Proteins - chemistry
14-3-3 Proteins - genetics
14-3-3 Proteins - metabolism
Alternative Splicing
Amino Acid Sequence
APOPTOSIS
BIOLOGICAL RADIATION EFFECTS
Cell survival
Conserved Sequence
DIMERIZATION
DIMERS
Exons - genetics
Humans
IRRADIATION
Molecular Sequence Data
Monomer
MONOMERS
Protein Multimerization
Protein Structure, Secondary
Protein Structure, Tertiary
PROTEINS
RADIATION, THERMAL, AND OTHER ENVIRONMENTAL POLLUTANT EFFECTS ON LIVING ORGANISMS AND BIOLOGICAL MATERIALS
SPLICING
Splicing variant
Ultraviolet Rays
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2010.04.104