p28, an anionic cell-penetrating peptide, increases the activity of wild type and mutated p53 without altering its conformation.
Mol Pharm
; 10(9): 3375-83, 2013 Sep 03.
Article
em En
| MEDLINE
| ID: mdl-23952735
ABSTRACT
p28, a cell penetrating peptide, binds to the DNA binding domain (DBD) of p53, inducing a post-translational increase in intracellular levels of wild type and mutant p53 activating pathways that inhibit cancer cell proliferation at G2/M. Cancer cells respond to p28 with an increase in p53 activity, except when mutations either alter DNA contact or completely unfold the DBD. The increase in p53 activity is accompanied by a significant reduction in the level of the E3 ligase COP1, with no alteration in p53 conformation. This suggests p28 can activate p53 over a wide range of conformational mutations by inhibiting the binding of COP1 to p53.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteína Supressora de Tumor p53
/
Peptídeos Penetradores de Células
Limite:
Humans
Idioma:
En
Revista:
Mol Pharm
Assunto da revista:
BIOLOGIA MOLECULAR
/
FARMACIA
/
FARMACOLOGIA
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
Estados Unidos