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

Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
Mitogens and the Cell Cycle02:38

Mitogens and the Cell Cycle

Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...

You might also read

Related Articles

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

Sort by
Same author

Gradual consolidation of skilled sequential movements in primary motor cortex of non-human primates.

bioRxiv : the preprint server for biology·2026
Same author

Attachment insecurity, adverse childhood experiences (ACEs), and suicidality in French residential-care adolescents: a gender-differentiated study.

Child and adolescent psychiatry and mental health·2025
Same author

Visual Recovery Reflects Cortical MeCP2 Sensitivity in Rett Syndrome.

Annals of clinical and translational neurology·2025
Same author

SUMOylation of nuclear receptor Nor1/NR4A3 coordinates microtubule cytoskeletal dynamics and stability in neuronal cells.

Cell & bioscience·2024
Same author

Clinical characteristics, course and prognosis of Multiple Sclerosis patients with epilepsy. A case control study: MS and epilepsy.

Multiple sclerosis and related disorders·2024
Same author

Differential Regulation of POC5 by ERα in Human Normal and Scoliotic Cells.

Genes·2023

Related Experiment Video

Updated: Jun 19, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
09:07

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Published on: December 19, 2018

Challenging estrogen receptor beta with phosphorylation.

Mélanie Sanchez1, Nathalie Picard, Karine Sauvé

  • 1Department of Biochemistry, Ste-Justine Hospital Research Center, University of Montreal, Montréal, Québec, Canada.

Trends in Endocrinology and Metabolism: TEM
|October 20, 2009
PubMed
Summary
This summary is machine-generated.

This review highlights estrogen receptor beta (ERbeta) functions and its signaling pathways. Understanding ERbeta

More Related Videos

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
15:05

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

Related Experiment Videos

Last Updated: Jun 19, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
09:07

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Published on: December 19, 2018

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
15:05

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

Area of Science:

  • Endocrinology and molecular biology
  • Nuclear hormone receptor signaling

Background:

  • Estrogen receptors (ERalpha and ERbeta) mediate diverse biological processes.
  • Estrogen's actions are well-studied for ERalpha, but ERbeta's role remains less understood.

Purpose of the Study:

  • To review current knowledge on estrogen receptor beta (ERbeta) function.
  • To explore the role of intracellular signals and protein phosphorylation in ERbeta activity.
  • To identify potential therapeutic targets for endocrine diseases affecting women's health.

Main Methods:

  • Literature review of estrogen receptor biology.
  • Analysis of signaling pathways impacting ERbeta.
  • Discussion of phosphorylation-mediated effects on ERbeta.

Main Results:

  • ERbeta plays significant roles in cellular communication and hormone responses.
  • Intracellular signals can elicit estrogen-like effects via ERbeta phosphorylation.
  • ERbeta's distinct functions from ERalpha are increasingly recognized.

Conclusions:

  • Further research into ERbeta function and its regulation is crucial.
  • Understanding cellular determinants of ERbeta action may reveal new treatment strategies.
  • Targeting ERbeta pathways holds promise for women's health and endocrine disease management.