JNK targets p53 ubiquitination and degradation in nonstressed cells
SY Fuchs, V Adler, T Buschmann, Z Yin… - Genes & …, 1998 - genesdev.cshlp.org
SY Fuchs, V Adler, T Buschmann, Z Yin, X Wu, SN Jones, Z Ronai
Genes & development, 1998•genesdev.cshlp.orgIn this study we elucidated the role of nonactive JNK in regulating p53 stability. The amount
of p53–JNK complex was inversely correlated with p53 level. A peptide corresponding to the
JNK binding site on p53 efficiently blocked ubiquitination of p53. Similarly, p53 lacking the
JNK binding site exhibits a longer half-life than p53wt. Outcompeting JNK association with
p53 increased the level of p53, whereas overexpression of a phosphorylation mutant form of
JNK inhibited p53 accumulation. JNK–p53 and Mdm2–p53 complexes were preferentially …
of p53–JNK complex was inversely correlated with p53 level. A peptide corresponding to the
JNK binding site on p53 efficiently blocked ubiquitination of p53. Similarly, p53 lacking the
JNK binding site exhibits a longer half-life than p53wt. Outcompeting JNK association with
p53 increased the level of p53, whereas overexpression of a phosphorylation mutant form of
JNK inhibited p53 accumulation. JNK–p53 and Mdm2–p53 complexes were preferentially …
In this study we elucidated the role of nonactive JNK in regulating p53 stability. The amount of p53–JNK complex was inversely correlated with p53 level. A peptide corresponding to the JNK binding site on p53 efficiently blocked ubiquitination of p53. Similarly, p53 lacking the JNK binding site exhibits a longer half-life than p53wt. Outcompeting JNK association with p53 increased the level of p53, whereas overexpression of a phosphorylation mutant form of JNK inhibited p53 accumulation. JNK–p53 and Mdm2–p53 complexes were preferentially found in G0/G1and S/G2M phases of the cell cycle, respectively. Altogether, these data indicate that JNK is an Mdm2-independent regulator of p53 stability in nonstressed cells.
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