Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Proteomic analysis identifies highly expressed plasma membrane proteins for detection and therapeutic targeting of specific breast cancer subtypes.

Clinical proteomics·2018
Same author

Integration of Breast Cancer Secretomes with Clinical Data Elucidates Potential Serum Markers for Disease Detection, Diagnosis, and Prognosis.

PloS one·2016
Same author

17β-Estradiol alters oxidative damage and oxidative stress response protein expression in the mouse mammary gland.

Molecular and cellular endocrinology·2016
Same author

Expression of estrogen receptor α in the mouse cerebral cortex.

Molecular and cellular endocrinology·2015
Same author

Nanopore-based assay for detection of methylation in double-stranded DNA fragments.

ACS nano·2015
Same author

17β-estradiol modulates gene expression in the female mouse cerebral cortex.

PloS one·2014
Same journal

Beyond fat storage: neuronal lipid droplets regulate whole-body metabolism.

Trends in endocrinology and metabolism: TEM·2026
Same journal

HDL resuscitates cells from ferroptosis.

Trends in endocrinology and metabolism: TEM·2026
Same journal

2-Methylbutyrylcarnitine (2MBC).

Trends in endocrinology and metabolism: TEM·2026
Same journal

Decoding growth hormone actions on human growth plate stem cells.

Trends in endocrinology and metabolism: TEM·2026
Same journal

Androgen loss backfires: Brain gate for tumor immunity.

Trends in endocrinology and metabolism: TEM·2026
Same journal

Glucocorticoid resistance-induced inflammation drives cardiovascular-kidney-metabolic (CKM) syndrome pathophysiology.

Trends in endocrinology and metabolism: TEM·2026
See all related articles

Related Experiment Video

Updated: Jun 3, 2026

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
07:28

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

ERα-associated protein networks.

Jennifer R Schultz-Norton1, Yvonne S Ziegler, Ann M Nardulli

  • 1Molecular and Integrative Physiology, University of Illinois at Urbana-Champaign, 407 South Goodwin Avenue, Urbana, IL 61801, USA.

Trends in Endocrinology and Metabolism: TEM
|March 5, 2011
PubMed
Summary
This summary is machine-generated.

Estrogen receptor alpha (ERα) acts as a scaffold, recruiting protein networks to regulate gene expression and DNA repair. These complexes are crucial for receptor function and cellular maintenance.

More Related Videos

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
06:01

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

Related Experiment Videos

Last Updated: Jun 3, 2026

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
07:28

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
06:01

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Estrogen receptor alpha (ERα) is a key transcription factor activated by hormones.
  • Previously, ERα was thought to interact with individual proteins.
  • Emerging evidence highlights ERα's role in recruiting protein complexes.

Purpose of the Study:

  • To elucidate the role of protein networks recruited by ERα.
  • To understand how these networks influence ERα function and gene expression.
  • To explore ERα's involvement in cellular repair mechanisms.

Main Methods:

  • Literature review of studies on ERα interactions.
  • Analysis of protein recruitment dynamics.
  • Investigation of ERα's role in DNA repair and oxidative stress response.

Main Results:

  • ERα recruits interconnected protein networks, not just individual proteins.
  • These networks are vital for ERα structure, DNA binding, and gene regulation.
  • ERα acts as a nucleating factor for complexes involved in DNA repair and oxidative stress response.

Conclusions:

  • ERα's function extends beyond simple transcription factor activity.
  • Protein networks recruited by ERα are essential for maintaining cellular homeostasis.
  • ERα plays a central role in coordinating responses to DNA damage and oxidative stress.