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Phosphorylation of estrogen receptor alpha, serine residue 305 enhances activity.

Molecular and cellular endocrinology - 25 Nov 2008

Tharakan Robin, Lepont Pierig, Singleton David, Kumar Rakesh, Khan Sohaib

Abstract excerpt

Upon ligand binding the estrogen receptor alters its conformation, dimerizes, binds to estrogen response elements (EREs), recruits cofactors and initiates the formation of a transcriptional complex. In addition to estradiol binding, hormone receptor activity is modulated by phosphorylation at several key residues. Previous studies have shown that p21-activated kinase-1 (Pak1) and cyclic-AMP dependent protein...

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Identifiers

PMID: 18755239
DOI: 10.1016/j.mce.2008.07.018

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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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