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Article

Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1.

Molecular cell - 1 Apr 1999

Tremblay A, Tremblay G B, Labrie F, Giguère V

Abstract excerpt

The estrogen receptors (ERs) alpha and beta possess a constitutive N-terminal activation function (AF-1) whose activity can be modulated by kinase signalling pathways. We demonstrate here that phosphorylation of AF-1 by MAP kinase (MAPK) leads to the recruitment of steroid receptor coactivator-1 (SRC-1) by ER beta in vitro. Enhancement of the interaction between SRC-1 and ER beta AF-1 is also observed in vivo in...

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Source

Identifiers

PMID: 10230404
DOI: 10.1016/s1097-2765(00)80479-7

Genes

SRC
EGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1.PMID 10230404Read ↗

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Selective recognition of distinct classes of coactivators by a ligand-inducible activation domain.Semantic proximity Read ↗

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The estrogen receptor enhances AP-1 activity by two distinct mechanisms with different requirements for receptor transactivation functions.Semantic proximity Read ↗

Synergism between ERalpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains.Semantic proximity Read ↗

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The Function of Steroid Receptor Coactivator-1 in Normal Tissues and CancerSemantic proximity Read ↗

An antiestrogen-responsive estrogen receptor-alpha mutant (D351Y) shows weak AF-2 activity in the presence of tamoxifen.Semantic proximity Read ↗

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