Abstract
The anti-apoptotic protein, Bcl-2 was phosphorylated at the Ser-87 residue in normal human blood cells, while it was not phosphorylated in tumor cells. We identified protein phosphatase 2A (PP2A) as a Bcl-2-associated phosphatase that is responsible for dephosphorylation of Bcl-2 in tumor cell lines. Treatment of the tumor cells with a PP2A inhibitor resulted in the appearance of Bcl-2 phosphorylation at Ser-87. This observation suggests that Bcl-2 is constitutively phosphorylated, but is immediately dephosphorylated by PP2A in tumors. Phosphorylation of Bcl-2 protein at the Ser-87 residue resulted in a reduction in anti-apoptotic function in human tumor cell lines. Thus, not only the expression level, but also the dephosphorylation status may have important implications for the oncogenic activity of Bcl-2.
| Original language | English |
|---|---|
| Pages (from-to) | 266-270 |
| Number of pages | 5 |
| Journal | Cancer Science |
| Volume | 95 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2004 Mar |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Cancer Research
- Oncology
Cite this
Dephosphorylation of Bcl-2 by protein phosphatase 2A results in apoptosis resistance. / Simizu, Siro; Tamura, Yuki; Osada, Hiroyuki.
In: Cancer Science, Vol. 95, No. 3, 03.2004, p. 266-270.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Dephosphorylation of Bcl-2 by protein phosphatase 2A results in apoptosis resistance
AU - Simizu, Siro
AU - Tamura, Yuki
AU - Osada, Hiroyuki
PY - 2004/3
Y1 - 2004/3
N2 - The anti-apoptotic protein, Bcl-2 was phosphorylated at the Ser-87 residue in normal human blood cells, while it was not phosphorylated in tumor cells. We identified protein phosphatase 2A (PP2A) as a Bcl-2-associated phosphatase that is responsible for dephosphorylation of Bcl-2 in tumor cell lines. Treatment of the tumor cells with a PP2A inhibitor resulted in the appearance of Bcl-2 phosphorylation at Ser-87. This observation suggests that Bcl-2 is constitutively phosphorylated, but is immediately dephosphorylated by PP2A in tumors. Phosphorylation of Bcl-2 protein at the Ser-87 residue resulted in a reduction in anti-apoptotic function in human tumor cell lines. Thus, not only the expression level, but also the dephosphorylation status may have important implications for the oncogenic activity of Bcl-2.
AB - The anti-apoptotic protein, Bcl-2 was phosphorylated at the Ser-87 residue in normal human blood cells, while it was not phosphorylated in tumor cells. We identified protein phosphatase 2A (PP2A) as a Bcl-2-associated phosphatase that is responsible for dephosphorylation of Bcl-2 in tumor cell lines. Treatment of the tumor cells with a PP2A inhibitor resulted in the appearance of Bcl-2 phosphorylation at Ser-87. This observation suggests that Bcl-2 is constitutively phosphorylated, but is immediately dephosphorylated by PP2A in tumors. Phosphorylation of Bcl-2 protein at the Ser-87 residue resulted in a reduction in anti-apoptotic function in human tumor cell lines. Thus, not only the expression level, but also the dephosphorylation status may have important implications for the oncogenic activity of Bcl-2.
UR - http://www.scopus.com/inward/record.url?scp=1842866996&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=1842866996&partnerID=8YFLogxK
U2 - 10.1111/j.1349-7006.2004.tb02214.x
DO - 10.1111/j.1349-7006.2004.tb02214.x
M3 - Article
VL - 95
SP - 266
EP - 270
JO - Cancer Science
JF - Cancer Science
SN - 1347-9032
IS - 3
ER -