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Cellular & Molecular Biology Letters

Open Access

SHP-2 and PTP-pest induction during Rb-E2F associated apoptosis

  • Liza D. Morales1, 3,
  • Karina Pena1,
  • Dae Joon Kim2, 3 and
  • Jonathan H. Lieman1Email author
Cellular & Molecular Biology LettersAn International Journal201217:20

Received: 25 October 2011

Accepted: 22 May 2012

Published: 29 May 2012


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.

Key words

ApoptosisFocal adhesion kinaseRbE2F-1PhosphatasePTP-1BSHP-2PTP-PESTPTPN1PTPN11PTPN12Tumor suppressor