Abstract:
:The role of the hormone prolactin (PRL) in the pathogenesis of breast cancer is mediated by its cognate receptor (PRLr). Ubiquitin-dependent degradation of the PRLr that negatively regulates PRL signaling is triggered by PRL-mediated phosphorylation of PRLr on Ser349 followed by the recruitment of the beta-transducin repeats-containing protein (beta-TrCP) ubiquitin-protein isopeptide ligase. We report here for the first time that interaction between PRLr and beta-TrCP is less efficient in human breast cancer cells than in non-tumorigenic human mammary epithelial cells. Furthermore, we demonstrate that both PRLr degradation and PRLr phosphorylation on Ser349 are impaired in breast tumor cells and tissues, an observation that directly correlates with enhanced expression of the PRLr in malignant breast epithelium. These findings represent a novel mechanism through which altered PRLr stability may directly influence the pathogenesis of breast cancer.
journal_name
Oncogenejournal_title
Oncogeneauthors
Li Y,Clevenger CV,Minkovsky N,Kumar KG,Raghunath PN,Tomaszewski JE,Spiegelman VS,Fuchs SYdoi
10.1038/sj.onc.1209214subject
Has Abstractpub_date
2006-03-23 00:00:00pages
1896-902issue
13eissn
0950-9232issn
1476-5594pii
1209214journal_volume
25pub_type
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