Abstract
We previously reported that JNK is involved in the regulation of c-Myc-mediated apoptosis triggered by UV irradiation and anticancer drug treatment. Here we show that ASK1 is an upstream regulator for c-Myc-mediated apoptosis triggered by UV, and we found a direct role for Ser-62 and Ser-71 in the regulation of protein stability and function of c-Myc. The ASK1-JNK pathway enhanced the protein stability of c-Myc through phosphorylation at Ser-62 and Ser-71, which was required for c-Myc-dependent apoptosis by ASK1-signaling. Interestingly, ASK1-signaling attenuated the degradation of ubiquitinated c-Myc without affecting the ubiquitination process. Together, these findings indicate that the ASK1-JNK pathway promotes the proapoptotic activity of c-Myc by modulating c-Myc protein stability through phosphorylation at Ser-62 and Ser-71.
| Original language | English |
|---|---|
| Pages (from-to) | 1313-1320 |
| Number of pages | 8 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 281 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 2001 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
ASK1-signaling promotes c-Myc protein stability during apoptosis. / Noguchi, Kohji; Kokubu, Akiko; Kitanaka, Chifumi; Ichijo, Hidenori; Kuchino, Yoshiyuki.
In: Biochemical and Biophysical Research Communications, Vol. 281, No. 5, 2001, p. 1313-1320.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - ASK1-signaling promotes c-Myc protein stability during apoptosis
AU - Noguchi, Kohji
AU - Kokubu, Akiko
AU - Kitanaka, Chifumi
AU - Ichijo, Hidenori
AU - Kuchino, Yoshiyuki
PY - 2001
Y1 - 2001
N2 - We previously reported that JNK is involved in the regulation of c-Myc-mediated apoptosis triggered by UV irradiation and anticancer drug treatment. Here we show that ASK1 is an upstream regulator for c-Myc-mediated apoptosis triggered by UV, and we found a direct role for Ser-62 and Ser-71 in the regulation of protein stability and function of c-Myc. The ASK1-JNK pathway enhanced the protein stability of c-Myc through phosphorylation at Ser-62 and Ser-71, which was required for c-Myc-dependent apoptosis by ASK1-signaling. Interestingly, ASK1-signaling attenuated the degradation of ubiquitinated c-Myc without affecting the ubiquitination process. Together, these findings indicate that the ASK1-JNK pathway promotes the proapoptotic activity of c-Myc by modulating c-Myc protein stability through phosphorylation at Ser-62 and Ser-71.
AB - We previously reported that JNK is involved in the regulation of c-Myc-mediated apoptosis triggered by UV irradiation and anticancer drug treatment. Here we show that ASK1 is an upstream regulator for c-Myc-mediated apoptosis triggered by UV, and we found a direct role for Ser-62 and Ser-71 in the regulation of protein stability and function of c-Myc. The ASK1-JNK pathway enhanced the protein stability of c-Myc through phosphorylation at Ser-62 and Ser-71, which was required for c-Myc-dependent apoptosis by ASK1-signaling. Interestingly, ASK1-signaling attenuated the degradation of ubiquitinated c-Myc without affecting the ubiquitination process. Together, these findings indicate that the ASK1-JNK pathway promotes the proapoptotic activity of c-Myc by modulating c-Myc protein stability through phosphorylation at Ser-62 and Ser-71.
UR - http://www.scopus.com/inward/record.url?scp=0034805077&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034805077&partnerID=8YFLogxK
U2 - 10.1006/bbrc.2001.4498
DO - 10.1006/bbrc.2001.4498
M3 - Article
C2 - 11243879
AN - SCOPUS:0034805077
VL - 281
SP - 1313
EP - 1320
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 5
ER -