Estrogen receptor alpha (ERα) is a key mediator of estrogen actions in breast cancer cells. Understanding the effects of ligand-activated ERα in target cells requires identification of the molecular partners acting in concert with this nuclear receptor to transduce the hormonal signal. We applied Tandem Affinity Purification, glycerol gradient centrifugation and MS analysis to isolate and identify proteins interacting with ligand-activated ERα in MCF-7 cell nuclei. This led to the identification of 264 ER-associated proteins, whose functions highlight the hinge role of ERα in coordination of multiple hormone-regulated nuclear processes in breast cancer cells.
Identification of proteins associated with ligand-activated estrogen receptor α in human breast cancer cell nuclei by tandem affinity purification and nano LC-MS/MS.
NOLA, Ernesto;
2011
Abstract
Estrogen receptor alpha (ERα) is a key mediator of estrogen actions in breast cancer cells. Understanding the effects of ligand-activated ERα in target cells requires identification of the molecular partners acting in concert with this nuclear receptor to transduce the hormonal signal. We applied Tandem Affinity Purification, glycerol gradient centrifugation and MS analysis to isolate and identify proteins interacting with ligand-activated ERα in MCF-7 cell nuclei. This led to the identification of 264 ER-associated proteins, whose functions highlight the hinge role of ERα in coordination of multiple hormone-regulated nuclear processes in breast cancer cells.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
