Atypical regulation of SRC-3.

Abstract	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.
Authors	Michael J Garabedian, Susan K Logan
Journal	Trends in biochemical sciences (Trends Biochem Sci) Vol. 33 Issue 7 Pg. 301-4 (Jul 2008) ISSN: 0968-0004 [Print] England
PMID	18502645 (Publication Type: Journal Article)
Chemical References	Estrogen Receptor alpha Trans-Activators Histone Acetyltransferases NCOA3 protein, human Nuclear Receptor Coactivator 3 PKC-3 protein Protein Kinase C Proteasome Endopeptidase Complex
Topics	Animals Estrogen Receptor alpha (metabolism) Histone Acetyltransferases (metabolism) Humans Models, Biological Nuclear Receptor Coactivator 3 Phosphorylation Proteasome Endopeptidase Complex (metabolism) Protein Kinase C (metabolism) Trans-Activators (metabolism)

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