The multifunctional estrogen receptor-alpha F domain.
The members of the nuclear receptor superfamily act as transcriptional regulatory factors and exhibit a multidomain structure characterized as domains A-E/F. This review focuses on a small, relatively understudied region at the extreme carboxy-terminus of the estrogen receptor (ER) alpha, the F domain. The F domain contributes to differences in the activity of ER alpha and beta subtypes; it is required for tamoxifen's agonist activity on an estrogen response element, and it modifies the receptor's interactions with coregulators including steroid receptor coactivator-1. The differences between the F domains of the ER alpha and beta subtypes and among the other members of the nuclear hormone receptor superfamily may offer opportunities for selective control of the activity of these proteins.
Skafar
Debra F
DF
Department of Physiology, Wayne State University School of Medicine, 540 E. Canfield, Detroit, MI, 48201, USA. dskafar@med.wayne.edu
Zhao
Changqing
C
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D047628:Estrogen Receptor alpha / Q000737:chemistry* / Q000502:physiology*; D005786:Gene Expression Regulation / Q000502:physiology; D051557:Hepatocyte Nuclear Factor 4 / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D008024:Ligands; D008969:Molecular Sequence Data; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D017434:Protein Structure, Tertiary / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000378:metabolism
D047628:Estrogen Receptor alpha; C496592:HNF4A protein, human; D051557:Hepatocyte Nuclear Factor 4; D008024:Ligands; D014157:Transcription Factors