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SHP-2 and PTP-pest induction during Rb-E2F associated apoptosis
Cellular & Molecular Biology Letters volume 17, pages 422–432 (2012)
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.
Abbreviations
- 4OHT:
-
4-hydroxytamoxifen
- dnE2F:
-
dominant negative mutant of E2F-1
- ER:
-
estrogen receptor
- FAK:
-
focal adhesion kinase
- PTP:
-
protein tyrosine phosphatase
- PTP-PEST:
-
protein tyrosine phosphatase rich in proline, glutamic acid/aspartic acid, and serine/threonine residues
- Rb:
-
retinoblastoma protein
- SHP-2:
-
SH2 domain-containing tyrosine phosphatase
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Morales, L.D., Pena, K., Kim, D.J. et al. SHP-2 and PTP-pest induction during Rb-E2F associated apoptosis. Cell Mol Biol Lett 17, 422–432 (2012). https://doi.org/10.2478/s11658-012-0020-9
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DOI: https://doi.org/10.2478/s11658-012-0020-9