The Phosphorylated Estrogen Receptor α (ER) Cistrome Identifies a Subset of Active Enhancers Enriched for Direct ER-DNA Binding and the Transcription Factor GRHL2-Reference-Cited by-同舟云学术

The Phosphorylated Estrogen Receptor α (ER) Cistrome Identifies a Subset of Active Enhancers Enriched for Direct ER-DNA Binding and the Transcription Factor GRHL2

Published:2019-02 Issue:3 Volume:39 Page:
ISSN:0270-7306
Container-title:Molecular and Cellular Biology
language:en
Short-container-title:Mol Cell Biol

Author:

Helzer Kyle T.¹^ORCID,Szatkowski Ozers Mary¹²,Meyer Mark B.³,Benkusky Nancy A.³,Solodin Natalia¹,Reese Rebecca M.¹,Warren Christopher L.²,Pike J. Wesley³,Alarid Elaine T.¹

Affiliation:

1. McArdle Laboratory for Cancer Research, Department of Oncology and Carbone Comprehensive Cancer Center, University of Wisconsin–Madison, Madison, Wisconsin, USA

2. Proteovista LLC, Madison, Wisconsin, USA

3. Department of Biochemistry, University of Wisconsin–Madison, Madison, Wisconsin, USA

Abstract

Posttranslational modifications are key regulators of protein function, providing cues that can alter protein interactions and cellular location. Phosphorylation of estrogen receptor α (ER) at serine 118 (pS118-ER) occurs in response to multiple stimuli and is involved in modulating ER-dependent gene transcription.

Funder

HHS | NIH | National Cancer Institute

HHS | National Institutes of Health

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

Link

https://journals.asm.org/doi/pdf/10.1128/MCB.00417-18

Reference99 articles.

1. Control of β-Catenin Phosphorylation/Degradation by a Dual-Kinase Mechanism

2. Protein-tyrosine kinases regulate the phosphorylation, protein interactions, subcellular distribution, and activity of p21ras GTPase-activating protein.