pRb controls Estrogen Receptor alpha protein stability and activity

A cross talk between the Estrogen Receptor (ESR1) and the Retinoblastoma (pRb) pathway has been demonstrated to influence the therapeutic response of breast cancer patients but the full mechanism remains poorly understood. Here we show that the N-terminal domain of pRb interacts with the CD domain o...

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Autores principales: Caligiuri, Isabella, Toffoli, Giuseppe, Giordano, Antonio, Rizzolio, Flavio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals LLC 2013
Materias:
Research Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3757244/
https://www.ncbi.nlm.nih.gov/pubmed/23900261
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author Caligiuri, Isabella
Toffoli, Giuseppe
Giordano, Antonio
Rizzolio, Flavio
author_facet Caligiuri, Isabella
Toffoli, Giuseppe
Giordano, Antonio
Rizzolio, Flavio
author_sort Caligiuri, Isabella
collection PubMed
description A cross talk between the Estrogen Receptor (ESR1) and the Retinoblastoma (pRb) pathway has been demonstrated to influence the therapeutic response of breast cancer patients but the full mechanism remains poorly understood. Here we show that the N-terminal domain of pRb interacts with the CD domain of ESR1 to allow for the assembly of intermediate complex chaperone proteins HSP90 and p23. We demonstrated that a loss of pRb in human/mouse breast cells decreases the expression of the ESR1 protein through the proteasome pathway. Our work reveals a novel regulatory mechanism of ESR1 basal turnover and activity and an unanticipated relationship with the pRb tumor suppressor.
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spelling pubmed-37572442013-09-03 pRb controls Estrogen Receptor alpha protein stability and activity Caligiuri, Isabella Toffoli, Giuseppe Giordano, Antonio Rizzolio, Flavio Oncotarget Research Papers A cross talk between the Estrogen Receptor (ESR1) and the Retinoblastoma (pRb) pathway has been demonstrated to influence the therapeutic response of breast cancer patients but the full mechanism remains poorly understood. Here we show that the N-terminal domain of pRb interacts with the CD domain of ESR1 to allow for the assembly of intermediate complex chaperone proteins HSP90 and p23. We demonstrated that a loss of pRb in human/mouse breast cells decreases the expression of the ESR1 protein through the proteasome pathway. Our work reveals a novel regulatory mechanism of ESR1 basal turnover and activity and an unanticipated relationship with the pRb tumor suppressor. Impact Journals LLC 2013-06-03 /pmc/articles/PMC3757244/ /pubmed/23900261 Text en Copyright: © 2013 Caligiuri et al. http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited
spellingShingle Research Papers
Caligiuri, Isabella
Toffoli, Giuseppe
Giordano, Antonio
Rizzolio, Flavio
pRb controls Estrogen Receptor alpha protein stability and activity
title pRb controls Estrogen Receptor alpha protein stability and activity
title_full pRb controls Estrogen Receptor alpha protein stability and activity
title_fullStr pRb controls Estrogen Receptor alpha protein stability and activity
title_full_unstemmed pRb controls Estrogen Receptor alpha protein stability and activity
title_short pRb controls Estrogen Receptor alpha protein stability and activity
title_sort prb controls estrogen receptor alpha protein stability and activity
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3757244/
https://www.ncbi.nlm.nih.gov/pubmed/23900261
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AT giordanoantonio prbcontrolsestrogenreceptoralphaproteinstabilityandactivity
AT rizzolioflavio prbcontrolsestrogenreceptoralphaproteinstabilityandactivity

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