Does palmitoylation target estrogen receptors to plasma membrane caveolae?

IUBMB Life. 2003 Jan;55(1):33-5. doi: 10.1080/1521654031000081256.

Abstract

The human nuclear estrogen receptors (i.e., ERalpha and ERbeta), as other transcriptional factors, regulate cellular processes inducing genomic events. In addition, the binding of 17beta-estradiol to ERs induces different membrane initiating non-genomic signaling. The non-genomic effects of ER are independent of transcriptional activity of the receptor and have been attributed to membrane ERs belonging to a signaling complex localized in caveolae. Here, we postulate that S-acylation of cysteine residue(s) present in the ligand binding domain of ERalpha and ERbeta may play a critical role in the membrane caveolar localization of the receptor and in the formation of the 'steroid signalosome'.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acylation
  • Amino Acid Sequence
  • Caveolae / chemistry
  • Caveolae / metabolism*
  • Humans
  • Molecular Sequence Data
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • Receptors, Estrogen / genetics
  • Receptors, Estrogen / metabolism*
  • Sequence Alignment

Substances

  • Protein Isoforms
  • Receptors, Estrogen

Associated data

  • SWISSPROT/P03372
  • SWISSPROT/Q03135
  • SWISSPROT/Q92731