title: Activation function 1 domain plays a negative role in dimerization of estrogen receptor beta.
abstract: Transcriptional potential of estrogen receptor beta (ERbeta) depends on the ligand binding and subsequent dimerization of the receptor protein. In order to examine the role of N-terminally located activation function 1 (AF-1) protein domain in the dimerization process of ERbeta, we used yeast SOS-Recruitment System (SRS). Two variants of ERbeta protein were expressed in the yeast cells: full length receptor and a truncated form, lacking AF-1. We observed that upon 17beta-estradiol treatment only the shorter form of the receptor dimerized, whereas the full-length one did not. This result suggests an inhibitory function of AF-1 in dimer formation and supports previous studies showing that N-terminal domain of ERbeta suppresses transcriptional activity.
authors.affiliation: Laboratory of Molecular Neurobiology, Nencki Institute of Experimental Biology, Pasteura 3, Warsaw 02-093, Poland.
authors.forename: Daniel
authors.initials: D
authors.lastname: Detka
authors.forename: Katarzyna
authors.initials: K
authors.lastname: Kalita
authors.forename: Leszek
authors.initials: L
authors.lastname: Kaczmarek
mesh_terms: D049109:Cell Proliferation / Q000187:drug effects; D019281:Dimerization; D004958:Estradiol / Q000494:pharmacology; D047629:Estrogen Receptor beta / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D009154:Mutation / Q000235:genetics; D017434:Protein Structure, Tertiary / Q000235:genetics / Q000502:physiology; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000235:genetics / Q000378:metabolism; D020664:Son of Sevenless Proteins / Q000235:genetics
chemical_list: D047629:Estrogen Receptor beta; D011993:Recombinant Fusion Proteins; D020664:Son of Sevenless Proteins; D004958:Estradiol