Abstract
Apoptosis is intimately connected to cell cycle regulation via the Retinoblastoma (Rb)-E2F pathway and thereby serves an essential role in tumor suppression by eliminating aberrant hyperproliferative cells. Upon loss of Rb activity, an apoptotic response can be elicited through both p53-dependent and p53-independent mechanisms. While much of this apoptotic response has been attributed to the p19ARF/p53 pathway, increasing evidence has supported the role of protein tyrosine phosphatases (PTPs) in contributing to the initiation of the Rb-E2F-associated apoptotic response. One protein tyrosine phosphatase, PTP-1B, which is induced by the Rb-E2F pathway, has been shown to contribute to a p53-independent apoptotic pathway by inactivating focal adhesion kinase. This report identifies two additional PTPs, SHP-2 and PTP-PEST, that are also directly activated by the Rb-E2F pathway and which can contribute to signal transduction during p53-independent apoptosis.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 422-432 |
| Number of pages | 11 |
| Journal | Cellular and Molecular Biology Letters |
| Volume | 17 |
| Issue number | 3 |
| DOIs | |
| State | Published - Sep 2012 |
Fingerprint
Keywords
- Apoptosis
- E2F-1
- Focal adhesion kinase
- Phosphatase
- PTP-1B
- PTP-PEST
- PTPN1
- PTPN11
- PTPN12
- Rb
- SHP-2
- Tumor suppressor
ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Molecular Biology
Cite this
SHP-2 and PTP-pest induction during Rb-E2F associated apoptosis. / Morales, Liza D.; Pena, Karina; Kim, Dae Joon; Lieman, Jonathan H.
In: Cellular and Molecular Biology Letters, Vol. 17, No. 3, 09.2012, p. 422-432.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - SHP-2 and PTP-pest induction during Rb-E2F associated apoptosis
AU - Morales, Liza D.
AU - Pena, Karina
AU - Kim, Dae Joon
AU - Lieman, Jonathan H.
PY - 2012/9
Y1 - 2012/9
N2 - Apoptosis is intimately connected to cell cycle regulation via the Retinoblastoma (Rb)-E2F pathway and thereby serves an essential role in tumor suppression by eliminating aberrant hyperproliferative cells. Upon loss of Rb activity, an apoptotic response can be elicited through both p53-dependent and p53-independent mechanisms. While much of this apoptotic response has been attributed to the p19ARF/p53 pathway, increasing evidence has supported the role of protein tyrosine phosphatases (PTPs) in contributing to the initiation of the Rb-E2F-associated apoptotic response. One protein tyrosine phosphatase, PTP-1B, which is induced by the Rb-E2F pathway, has been shown to contribute to a p53-independent apoptotic pathway by inactivating focal adhesion kinase. This report identifies two additional PTPs, SHP-2 and PTP-PEST, that are also directly activated by the Rb-E2F pathway and which can contribute to signal transduction during p53-independent apoptosis.
AB - Apoptosis is intimately connected to cell cycle regulation via the Retinoblastoma (Rb)-E2F pathway and thereby serves an essential role in tumor suppression by eliminating aberrant hyperproliferative cells. Upon loss of Rb activity, an apoptotic response can be elicited through both p53-dependent and p53-independent mechanisms. While much of this apoptotic response has been attributed to the p19ARF/p53 pathway, increasing evidence has supported the role of protein tyrosine phosphatases (PTPs) in contributing to the initiation of the Rb-E2F-associated apoptotic response. One protein tyrosine phosphatase, PTP-1B, which is induced by the Rb-E2F pathway, has been shown to contribute to a p53-independent apoptotic pathway by inactivating focal adhesion kinase. This report identifies two additional PTPs, SHP-2 and PTP-PEST, that are also directly activated by the Rb-E2F pathway and which can contribute to signal transduction during p53-independent apoptosis.
KW - Apoptosis
KW - E2F-1
KW - Focal adhesion kinase
KW - Phosphatase
KW - PTP-1B
KW - PTP-PEST
KW - PTPN1
KW - PTPN11
KW - PTPN12
KW - Rb
KW - SHP-2
KW - Tumor suppressor
UR - http://www.scopus.com/inward/record.url?scp=84863570315&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84863570315&partnerID=8YFLogxK
U2 - 10.2478/s11658-012-0020-9
DO - 10.2478/s11658-012-0020-9
M3 - Article
C2 - 22644489
AN - SCOPUS:84863570315
VL - 17
SP - 422
EP - 432
JO - Cellular and Molecular Biology Letters
JF - Cellular and Molecular Biology Letters
SN - 1425-8153
IS - 3
ER -