Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 59, Issue 5, Pages 821-831Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-002-8470-2
Keywords
estrogen receptor-alpha; regulation; splicing; isoform; tissue specificity; proteasome; post-translational modification; ubiquitination; phosphorylation; acetylation
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This review aims to evaluate the impact that human estrogen receptor-alpha (ER-alpha) synthesis, modification and degradation has on estrogen-dependant physiological and pathological processes within the body. Estrogen signaling is transduced through estrogen receptors, which act as ligand-inducible transcription factors. The significance of different isoforms of ER-alpha that lack structural features of full-length ER-alpha are discussed. The influence of differential promoter usage on the amount and isoform of ER-alpha within individual cell types is also reviewed. Moreover, the potential role of phosphorylation, ubiquitination and acetylation in the function and dynamic turnover of ER-alpha is presented.
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