Pin1 modulates ERα levels in breast cancer through inhibition of phosphorylation-dependent ubiquitination and degradation
Rajbhandari P, Schalper KA, Solodin NM, Ellison-Zelski SJ, Ping Lu K, Rimm DL, Alarid ET. Pin1 modulates ERα levels in breast cancer through inhibition of phosphorylation-dependent ubiquitination and degradation. Oncogene 2013, 33: 1438-1447. PMID: 23542176, PMCID: PMC3815749, DOI: 10.1038/onc.2013.78.Peer-Reviewed Original ResearchMeSH KeywordsBreast NeoplasmsCell Line, TumorEstrogen Receptor alphaFemaleHumansNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphorylationProteolysisUbiquitinationConceptsERα protein levelsERα proteinBreast cancerERα-positive breast cancerProtein levelsPotential surrogate markerRetrospective cohortSurrogate markerBreast carcinomaTherapy decisionsERα levelsESR1 levelsERα ubiquitinationCertain tumorsHuman tumorsDiscordant levelsESR1Pin1 levelsReceptor interactionUbiquitin-proteasome pathwayReceptor degradationImportant biomarkerTumorsCancerTransactivation function