HER2/HER3 heterodimers in prostate cancer

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HER2/HER3 heterodimers in prostate cancer Michael R. Freeman  Cancer Cell  Volume 6, Issue 5, Pages 427-428 (November 2004) DOI: 10.1016/j.ccr.2004.10.018

Figure 1 Activation of the androgen receptor (AR) as a result of HER2/HER3 dimerization HER/ErbB family receptor tyrosine kinases initiate intracellular signal transduction by dimerizing with each other or with other members of the receptor family. Signaling cascades originating from ErbB1/ErbB1 (1-1) and ErbB2/ErbB3 (2-3) dimers are shown, along with known protein intermediates. The Mellinghoff et al. (2004) study in this issue of Cancer Cell demonstrates the existence of a signal from the 2-3 dimer to the AR, resulting in enhancement of AR-dependent, hormone-independent signals. The paper presents evidence that the EGFR (participating in 1-1, 1-2, or 1-3 dimers) or the serine-threonine kinase Akt/protein kinase B, which lies downstream from the 2-3 dimer, are not involved in mediating this signaling mechanism. These findings indicate that targeting the 2-3 dimer specifically may be a promising means of therapeutic intervention in aggressive prostate cancer. The question mark indicates that the pathway from the 2-3 dimer to the AR was not identified. The ErbB3 icon has a cross in the cytoplasmic domain because the intrinsic kinase is inactive. NRG, neuregulin, a growth factor capable of activating the 2-3 dimer. Cancer Cell 2004 6, 427-428DOI: (10.1016/j.ccr.2004.10.018)