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Cellular and Molecular Life Sciences CMLS

, Volume 59, Issue 5, pp 821–831 | Cite as

Human estrogen receptor-α: regulation by synthesis, modification and degradation

  • G. Reid
  • S. Denger
  • M. Kos
  • F. Gannon

Abstract.

This review aims to evaluate the impact that human estrogen receptor-α (ER-α) 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-α that lack structural features of full-length ER-α are discussed. The influence of differential promoter usage on the amount and isoform of ER-α within individual cell types is also reviewed. Moreover, the potential role of phosphorylation, ubiquitination and acetylation in the function and dynamic turnover of ER-α is presented.

Key words. Estrogen receptor-α; regulation; splicing; isoform; tissue specificity; proteasome, post-translational modification; ubiquitination; phosphorylation; acetylation. 

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Copyright information

© Birkhäuser Verlag, 2002

Authors and Affiliations

  • G. Reid
    • 1
  • S. Denger
    • 1
  • M. Kos
    • 1
  • F. Gannon
    • 1
  1. 1.European Molecular Biology Laboratory, EMBL, Meyerhofstrasse 1, 69117 Heidelberg (Germany), Fax + 49 6221 8891202, e-mail: gannon@embo.orgDE

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