Title : Dihydrotestosterone induces p27 degradation via direct binding with SKP2 in ovarian and breast cancer.

Pub. Date : 2011 Jul

PMID : 21503567






8 Functional Relationships(s)
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1 Dihydrotestosterone induces p27 degradation via direct binding with SKP2 in ovarian and breast cancer. Dihydrotestosterone zinc ribbon domain containing 2 Homo sapiens
2 We found that DHT could down-regulate p27, but not p21, within 4 h. Further studies proved that DHT induced p27 degradation through the ubiquitin-proteasome proteolytic pathway. Dihydrotestosterone zinc ribbon domain containing 2 Homo sapiens
3 We found that DHT could down-regulate p27, but not p21, within 4 h. Further studies proved that DHT induced p27 degradation through the ubiquitin-proteasome proteolytic pathway. Dihydrotestosterone zinc ribbon domain containing 2 Homo sapiens
4 We found that DHT could down-regulate p27, but not p21, within 4 h. Further studies proved that DHT induced p27 degradation through the ubiquitin-proteasome proteolytic pathway. Dihydrotestosterone zinc ribbon domain containing 2 Homo sapiens
5 We found that DHT could down-regulate p27, but not p21, within 4 h. Further studies proved that DHT induced p27 degradation through the ubiquitin-proteasome proteolytic pathway. Dihydrotestosterone zinc ribbon domain containing 2 Homo sapiens
6 However, proteolysis inhibitors effectively antagonized the DHT-induced p27 degradation. Dihydrotestosterone zinc ribbon domain containing 2 Homo sapiens
7 DHT led to the direct binding of p27 to SKP2 independent of the phosphorylation status. Dihydrotestosterone zinc ribbon domain containing 2 Homo sapiens
8 Collectively, DHT, but not the other examined androgens regulated the degradation of p27 in MCF-7 and OVCAR-3 cells. Dihydrotestosterone zinc ribbon domain containing 2 Homo sapiens