HER2/HER3 heterodimers in prostate cancer: Whither HER1/EGFR?
In this issue of Cancer Cell, Mellinghoff et al. (2004) demonstrate that a small molecule inhibitor of the EGF receptor (EGFR) and the HER2/ErbB2/c-Neu kinase blocks signaling to the androgen receptor by a mechanism that involves HER2/HER3 heterodimerization. Surprisingly, the EGFR is peripheral to this signaling mechanism. These results have implications for the design of targeted therapy for hormone-refractory prostate cancer.
Freeman
Michael R
MR
Urological Diseases Research Center, Children's Hospital Boston, Harvard Medical School, Enders Research Laboratories, Suite 1161, 300 Longwood Avenue, Boston, Massachusetts 02115, USA. michael.freeman@childrens.harvard.edu
D019281:Dimerization; D066246:ErbB Receptors / Q000502:physiology*; D006801:Humans; D008297:Male; D008954:Models, Biological; D009376:Neoplasms, Hormone-Dependent / Q000378:metabolism; D011471:Prostatic Neoplasms / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D051057:Proto-Oncogene Proteins c-akt; D018719:Erb-b2 Receptor Tyrosine Kinases / Q000502:physiology*; D020893:Receptor, ErbB-3 / Q000502:physiology*; D011944:Receptors, Androgen / Q000378:metabolism
D066246:ErbB Receptors; D017346:Protein Serine-Threonine Kinases; D011518:Proto-Oncogene Proteins; D051057:Proto-Oncogene Proteins c-akt; D018719:Erb-b2 Receptor Tyrosine Kinases; D020893:Receptor, ErbB-3; D011944:Receptors, Androgen