Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Actin Filament Depolymerization

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...

Mechanism of Filopodia Formation

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...

Amplifying Signals via Enzymatic Cascade

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...

Calmodulin-dependent Signaling

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...

Intracellular Signaling Affects Focal Adhesions

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...

MAPK Signaling Cascades

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...

You might also read

Related Articles

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

Sort by

Same author

Both Nuclear and Membrane Estrogen Receptor Alpha Impact the Expression of Estrogen Receptors and Plasticity Markers in the Mouse Hypothalamus and Hippocampus.

Biology·2023

Same author

Sleep Deprivation and Circadian Disruption Stress, Allostasis, and Allostatic Load.

Sleep medicine clinics·2022

Same author

Sex and chronic stress alter the distribution of glutamate receptors within rat hippocampal CA3 pyramidal cells following oxycodone conditioned place preference.

Neurobiology of stress·2022

Same author

Corticosterone induces discrete epigenetic signatures in the dorsal and ventral hippocampus that depend upon sex and genotype: focus on methylated Nr3c1 gene.

Translational psychiatry·2022

Same author

Genomic modules and intramodular network concordance in susceptible and resilient male mice across models of stress.

Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology·2021

Same author

Acute Delta 9-tetrahydrocannabinol administration differentially alters the hippocampal opioid system in adult female and male rats.

Synapse (New York, N.Y.)·2021

Search research articles

Related Experiment Video

Updated: Jun 10, 2026

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

LIM kinase mediates estrogen action on the actin depolymerization factor Cofilin.

Genevieve S Yuen¹, Bruce S McEwen, Keith T Akama

¹Harold and Margaret Milliken Hatch Laboratory of Neuroendocrinology, The Rockefeller University, New York, NY 10065-6399, USA.

|August 11, 2010

Summary

This summary is machine-generated.

Estrogen enhances brain synapse connections in young rats by activating Cofilin via LIM kinase, a process impaired in aged brains, impacting neuronal morphology and actin cytoskeleton reorganization.

More Related Videos

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

Published on: April 14, 2023

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

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

Published on: December 19, 2018

Related Experiment Videos

Last Updated: Jun 10, 2026

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

Published on: April 14, 2023

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

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

Published on: December 19, 2018

Area of Science:

Neuroscience
Cell Biology
Endocrinology

Background:

Estrogen influences synaptic plasticity in the hippocampus, with effects diminishing in aged female rats.
Estrogen-mediated synapse changes involve actin cytoskeleton reorganization, requiring Cofilin deactivation.
Cofilin deactivation is regulated by LIM kinase (LIMK) phosphorylation, a process affected by aging.

Purpose of the Study:

To investigate if estrogen's effect on synapse density is mediated by Cofilin.
To determine if estrogen's action on Cofilin requires LIMK activity.
To explore estrogen's role in actin-dependent neuronal morphology.

Main Methods:

In vitro studies using hippocampal neurons and NG108-15 neuroblastoma cells.
Assessing estrogen's effect on Cofilin phosphorylation.
Evaluating the requirement of LIMK in estrogen-induced Cofilin phosphorylation.
Observing estrogen's impact on neuronal morphology and filopodial extensions.

Main Results:

Estrogen stimulates Cofilin phosphorylation in vitro.
Estrogen's action on Cofilin phosphorylation is dependent on LIMK activity.
Estrogen promotes filopodial extensions, indicating altered actin-dependent neuronal morphology.
Estrogen links to Cofilin via LIMK, explaining age-related changes in pLIMK-IR.

Conclusions:

Estrogen modulates neuronal actin cytoskeleton dynamics through the LIMK-Cofilin pathway.
This pathway is crucial for estrogen's effects on synaptic structure and neuronal morphology.
The findings provide a functional link between estrogen signaling, actin dynamics, and age-related cognitive decline.