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

Regulation of Nuclear Protein Sorting

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...

NF-κB-dependent Signaling Pathway

NF-κB-dependent Signaling Pathway

The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
The...

Regulation of the Unfolded Protein Response

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...

Transducer Mechanism: Nuclear Receptors

Transducer Mechanism: Nuclear Receptors

Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:

You might also read

Related Articles

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

Sort by

Same author

MSC-derived extracellular vesicles accelerate wound healing in senescent fibroblast cultures.

Biogerontology·2026

Same author

Mutagen-induced somatic mutation rate in primary mammalian cells in relation to maximum life span.

Geromedicine·2026

Same author

Long-lived mammals contain more phosphorylation sites in the SIRT6 C-terminus that enhance PARP1 interaction and resistance to oxidative stress.

bioRxiv : the preprint server for biology·2026

Same author

Replacement-Based Ageing Interventions for Systemic Rejuvenation: Shaping Longevity Science and Clinical Directions.

Aging cell·2026

Same author

Comparative analysis of naked mole-rat thermogenesis and its potential to maintain euthermia in response to cold.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Toward actionable interventions in human aging (12th ARDD meeting, 2025).

Aging·2026

Same journal

Co-option of lysosomal machinery shapes the evolution of the intracellular photosymbiosis supporting coral reefs.

Cell·2026

Same journal

LEF1 and niche factors determine T cell stemness across chronic diseases.

Cell·2026

Same journal

Recurrent patterns of TOP1-mediated neuronal genomic damage shared by major neurodegenerative disorders.

Cell·2026

Same journal

Four-dimensional molecular mapping from a spatial snapshot reveals the dynamics of hair follicle organogenesis.

Cell·2026

Same journal

Whole-cell particle-based digital twin simulations from 4D lattice light-sheet microscopy data.

Cell·2026

Same journal

Systematic discovery of pathogen effector functions across human pathogens and pathways.

Cell·2026

See all related articles

Search research articles

Related Experiment Video

Updated: May 5, 2026

Capture and Identification of RNA-binding Proteins by Using Click Chemistry-assisted RNA-interactome Capture CARIC Strategy

Capture and Identification of RNA-binding Proteins by Using Click Chemistry-assisted RNA-interactome Capture CARIC Strategy

Published on: October 19, 2018

Dangerous Entrapment for NRF2.

Vera Gorbunova¹, Sarallah Rezazadeh¹, Andrei Seluanov¹

¹Department of Biology, 434 Hutchison Hall, River Campus, University of Rochester, Rochester, NY 14627, USA.

|June 4, 2016

Summary

This summary is machine-generated.

Progerin protein causes Hutchinson-Gilford progeria (HGPS) by trapping the NRF2 protein at the cell nucleus. This impairs cellular defense, leading to oxidative stress and premature aging.

More Related Videos

Measurements of Physiological Stress Responses in C. Elegans

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Published on: May 9, 2020

Related Experiment Videos

Last Updated: May 5, 2026

Capture and Identification of RNA-binding Proteins by Using Click Chemistry-assisted RNA-interactome Capture CARIC Strategy

Capture and Identification of RNA-binding Proteins by Using Click Chemistry-assisted RNA-interactome Capture CARIC Strategy

Published on: October 19, 2018

Measurements of Physiological Stress Responses in C. Elegans

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Published on: May 9, 2020

Area of Science:

Cell Biology
Genetics
Molecular Medicine

Background:

Hutchinson-Gilford progeria (HGPS) is a rare, fatal genetic disorder characterized by premature aging.
The condition is caused by mutations in the LMNA gene, leading to the production of a toxic protein called progerin.
Progerin accumulates in the nuclear envelope, disrupting nuclear structure and function.

Purpose of the Study:

To elucidate the molecular mechanism by which progerin drives HGPS pathogenesis.
To investigate the role of the transcription factor NRF2 in progerin-induced cellular dysfunction.
To identify potential therapeutic targets for HGPS.

Main Methods:

Cellular and biochemical assays were used to examine progerin-NRF2 interactions.
Immunofluorescence microscopy was employed to visualize the localization of progerin and NRF2 in HGPS cells.
Analysis of NRF2 signaling pathway activation and oxidative stress markers.

Main Results:

Progerin directly binds to and sequesters NRF2 at the nuclear periphery in HGPS cells.
This sequestration prevents NRF2 from translocating to the nucleus and activating its target genes.
Impaired NRF2 signaling leads to reduced antioxidant defense and increased oxidative stress.

Conclusions:

Progerin-induced trapping of NRF2 at the nuclear periphery is a key mechanism driving HGPS.
Targeting progerin-NRF2 interactions or restoring NRF2 function may offer therapeutic strategies for HGPS.