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

Restarting Stalled Replication Forks

Restarting Stalled Replication Forks

DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart, a...

Non-Canonical Wnt Signaling Pathways

Non-Canonical Wnt Signaling Pathways

Wnt is a zygotic effect gene that is expressed during very early embryonic development. It regulates various processes in animals starting from early development through the adult stage, such as organogenesis in the embryo and maintenance of neuronal and blood stem cells. Wnt proteins can induce a wide variety of intracellular pathways depending upon the specific abilities of different Wnt ligands to form a complex with shared and cognate receptors in the presence of different co-receptors. The...

Canonical Wnt Signaling Pathway

Canonical Wnt Signaling Pathway

The gene encoding the main signaling molecules of the Wnt signaling pathways (the Wnt proteins) was discovered almost four decades ago by Nüsslein-Volhard and Wieschaus. They identified and originally named the gene "wingless" (wg) after a phenotype discovered during their landmark genetic screen in Drosophila for body pattern defects. At around the same time, another researcher named Harold Varmus found that a murine tumor virus activates the mammalian wg homolog, Int-1, which results in tumor...

Canonical Wnt Signaling Pathway

Canonical Wnt Signaling Pathway

The gene encoding the main signaling molecules of the Wnt signaling pathways (the Wnt proteins) was discovered almost four decades ago by Nüsslein-Volhard and Wieschaus. They identified and originally named the gene "wingless" (wg) after a phenotype discovered during their landmark genetic screen in Drosophila for body pattern defects. At around the same time, another researcher named Harold Varmus found that a murine tumor virus activates the mammalian wg homolog, Int-1, which results in tumor...

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...

Mechanism of Lamellipodia Formation

Mechanism of Lamellipodia Formation

Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...

You might also read

Related Articles

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

Sort by

Same author

TOP1 and TOP2 complementarily maintain DNA replication fork progression in vertebrates.

The Journal of biological chemistry·2026

Same author

Rad18 suppresses the late step of human immunodeficiency virus type 1 replication.

bioRxiv : the preprint server for biology·2025

Same author

Functions of a subunit of DNA polymerase δ, POLD3, revealed by depletion of WRNIP1.

Biochemical and biophysical research communications·2025

Same author

Overexpression of CDT1 inhibits cell cycle progression at S phase by interacting with the mini-chromosome maintenance complex and causes DNA damage.

FEBS open bio·2025

Same author

ST2<sup>+</sup> effector memory helper T cells are responsible for long-term asthma exacerbation leading to female-predominant airway inflammation.

Allergology international : official journal of the Japanese Society of Allergology·2025

Same author

TIPIN is essential for chromosome stability and cell viability in BRCA1-deficient cells.

Biochemical and biophysical research communications·2025

Search research articles

Related Experiment Video

Updated: Jun 22, 2026

A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases

A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases

Published on: December 23, 2013

Physical and functional interaction between WRNIP1 and RAD18.

Akari Yoshimura¹, Masayuki Seki, Makoto Kanamori

¹Molecular Cell Biology Laboratory, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan. seki@mail.pharm.tohoku.ac.jp

Genes & Genetic Systems

|June 27, 2009

Summary

Human WRNIP1 protein binds to DNA, interacting with RAD18. This interaction influences RAD18

More Related Videos

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51

Published on: February 13, 2019

Related Experiment Videos

Last Updated: Jun 22, 2026

A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases

A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases

Published on: December 23, 2013

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51

Published on: February 13, 2019

Area of Science:

Molecular Biology
Genetics
DNA Repair Mechanisms

Background:

WRNIP1 (WRN interacting protein 1) is a conserved protein interacting with WRN.
Yeast studies suggest WRNIP1's ortholog (Mgs1) functions in DNA damage tolerance pathways.
These pathways are distinct from established template-switch damage avoidance mechanisms.

Purpose of the Study:

To investigate the DNA binding properties of human WRNIP1.
To elucidate the interaction between WRNIP1 and RAD18 in DNA binding.
To understand WRNIP1's role in DNA damage tolerance pathways.

Main Methods:

Biochemical assays to test ATP-dependent DNA binding of WRNIP1.
Co-immunoprecipitation to confirm physical interaction between WRNIP1 and RAD18.
DNA binding assays to assess the effect of WRNIP1-RAD18 interaction on DNA binding.

Main Results:

Human WRNIP1 binds to forked DNA (mimicking stalled replication forks) and template/primer DNA in an ATP-dependent manner.
WRNIP1 physically interacts with RAD18.
WRNIP1 interferes with RAD18 binding to DNA, while RAD18 enhances WRNIP1's DNA binding, indicating WRNIP1 targets RAD18-bound DNA.

Conclusions:

WRNIP1 plays a role in DNA damage tolerance by interacting with RAD18.
The interplay between WRNIP1 and RAD18 suggests a coordinated mechanism for managing stalled replication forks.
WRNIP1's targeting of RAD18-bound DNA highlights its specific function within DNA repair pathways.