Atypical regulation of SRC-3.
Overexpression of steroid receptor coactivator 3 (SRC-3) is associated with an increased incidence of breast cancer. A recent study shows that SRC-3 is protected from proteasomal degradation by atypical protein kinase C (aPKC)-mediated phosphorylation in an estrogen receptor alpha (ERalpha)-dependent manner. This finding provides a novel mechanism for coupling increased SRC-3 expression with enhanced estrogen-dependent cellular proliferation.
Garabedian
Michael J
MJ
Department of Microbiology, and the New York University (NYU) Cancer Institute, NYU School of Medicine, 550 First Avenue, New York, NY 10016, USA. michael.garabedian@nyumc.org
Logan
Susan K
SK
D000818:Animals; D047628:Estrogen Receptor alpha / Q000378:metabolism*; D051548:Histone Acetyltransferases / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D056921:Nuclear Receptor Coactivator 3; D010766:Phosphorylation; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*; D015534:Trans-Activators / Q000378:metabolism*
D047628:Estrogen Receptor alpha; D015534:Trans-Activators; D051548:Histone Acetyltransferases; C538866:NCOA3 protein, human; D056921:Nuclear Receptor Coactivator 3; C115015:PKC-3 protein; D011493:Protein Kinase C; D046988:Proteasome Endopeptidase Complex