Premium
A mutant P53 can activate apoptosis through a mechanism distinct from those induced by wild type P53
Author(s) -
He Ming,
Rennie Paul S,
Dragowska Visia,
Nelson Colleen C,
Jia William
Publication year - 2002
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/s0014-5793(02)02609-1
Subject(s) - mutant , apoptosis , p53 protein , wild type , mutation , biology , dna , gene , amino acid , microbiology and biotechnology , chemistry , genetics
A common mutation in P53 protein occurs at amino acid residue 281 in the DNA binding domain (P53 gly(281) ), which results in loss of transcriptional regulation of P53 target genes and has been reported to gain pro‐oncogenic functions. In the present study, we investigated the activity of P53 gly(281) in P53‐null PC3 human prostate cancer cells and found that the P53 gly(281) induced apoptosis as efficiently as the wild‐type P53 (wtP53). However, in contrast to wtP53‐induced apoptosis, the P53 gly(281) ‐induced apoptosis was insensitive to overexpression of bcl‐2. Thus, our findings indicate that while a mutation in the DNA binding domain of p53 may result in a more oncogenic form of the protein, it may also paradoxically result in the ‘gain’ of a new, alternative pathway for apoptosis.