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Leucine zipper‐like domain is required for tumor suppressor ING2‐mediated nucleotide excision repair and apoptosis
Author(s) -
Wang Yemin,
Wang Jing,
Li Gang
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.05.065
Subject(s) - leucine zipper , microbiology and biotechnology , chromatin , bzip domain , zipper , suppressor , chromatin remodeling , apoptosis , scaffold protein , cancer research , chemistry , chromatin structure remodeling (rsc) complex , dna , biology , signal transduction , transcription factor , biochemistry , gene , algorithm , computer science
The plant homodomain (PHD) of ING2 was shown to regulate p53‐dependent apoptosis through phosphoinositides signaling. However, the role of a predicted leucine zipper‐like (LZL) motif in N‐terminus of ING2 is unclear. Here, we show that LZL motif is critical for the proper functions of ING2 in DNA repair, apoptosis and chromatin remodeling after UV irradiation. Deletion of LZL domain also abrogated the association between ING2 and p53, but not between ING2 and p300, suggesting that ING2 modulates p53‐dependent chromatin remodeling, apoptosis and DNA repair by functioning as a scaffold protein to mediate the interaction between p53 and p300.