Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor.
Ontology highlight
ABSTRACT:
SUBMITTER: Tateishi Y
PROVIDER: S-EPMC535086 | biostudies-other | 2004 Dec
REPOSITORIES: biostudies-other
Publications
Ligand-dependent switching of ubiquitin-proteasome pathways for estrogen receptor.
Tateishi Yukiyo Y Kawabe Yoh-ichi Y Chiba Tomoki T Murata Shigeo S Ichikawa Ken K Murayama Akiko A Tanaka Keiji K Baba Tadashi T Kato Shigeaki S Yanagisawa Junn J
The EMBO journal 20041111 24
Recent evidence indicates that the transactivation of estrogen receptor alpha (ERalpha) requires estrogen-dependent receptor ubiquitination and degradation. Here we show that estrogen-unbound (unliganded) ERalpha is also ubiquitinated and degraded through a ubiquitin-proteasome pathway. To investigate this ubiquitin-proteasome pathway, we purified the ubiquitin ligase complex for unliganded ERalpha and identified a protein complex containing the carboxyl terminus of Hsc70-interacting protein (CH ...[more]
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