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

Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.2K
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...
3.2K
DNA Damage can Stall the Cell Cycle02:37

DNA Damage can Stall the Cell Cycle

9.3K
In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
9.3K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

3.0K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
3.0K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

5.5K
Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
5.5K
Actin Polymerization01:42

Actin Polymerization

7.0K
Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶  nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
7.0K
Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

5.9K
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,...
5.9K

You might also read

Related Articles

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

Sort by
Same author

Multifaceted roles of PDS5B in RAD51-dependent homology-directed DNA repair and replication fork protection.

Nature communications·2026
Same author

Structural insight into how RAD51 paralog exchange regulates RAD51 filament formation.

Nature structural & molecular biology·2026
Same author

Structural basis for the mechanism and stability of the EEPD1 5' endonuclease.

The Journal of biological chemistry·2026
Same author

Resolution of R-loops and transcription-replication conflicts by SETX-BRCA1-BARD1 complex.

Nature structural & molecular biology·2026
Same author

Author Correction: Structural insights into BCDX2 complex function in homologous recombination.

Nature·2026
Same author

Antibody-Mediated Targeting of Secretory Protein SCUBE3 Suppresses Cancer Progression by Inhibiting Oncogenic Signaling and Inducing Antitumor Immunity.

Cancer research·2025

Related Experiment Video

Updated: Sep 17, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

8.1K

The DNA Repair Component EEPD1 Regulates Actin Polymerization.

Robert Hromas1, Austin Kirby1, Andrew Carrillo1

  • 1Division of Hematology and Medical Oncology, Department of Medicine and the Mays Cancer Center, University of Texas Health Science Center, San Antonio, Texas, USA.

Biology of the Cell
|July 1, 2025
PubMed
Summary

Endonuclease exonuclease phosphatase domain-containing protein 1 (EEPD1) regulates cell migration and nuclear shape by controlling actin polymerization. This protein links DNA repair to cytoskeletal organization.

Keywords:
EEPD1actincell membranecell migration

More Related Videos

Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage
10:44

Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage

Published on: January 31, 2018

10.4K
Visualization of DNA Repair Proteins Interaction by Immunofluorescence
07:55

Visualization of DNA Repair Proteins Interaction by Immunofluorescence

Published on: June 26, 2020

10.4K

Related Experiment Videos

Last Updated: Sep 17, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

8.1K
Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage
10:44

Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage

Published on: January 31, 2018

10.4K
Visualization of DNA Repair Proteins Interaction by Immunofluorescence
07:55

Visualization of DNA Repair Proteins Interaction by Immunofluorescence

Published on: June 26, 2020

10.4K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Endonuclease exonuclease phosphatase domain-containing protein 1 (EEPD1) is a DNA repair enzyme.
  • EEPD1 undergoes post-translational modifications like myristoylation and palmitoylation in response to cholesterol.
  • Its role beyond DNA repair was not well understood.

Purpose of the Study:

  • To investigate the non-DNA repair functions of EEPD1.
  • To explore EEPD1's role in cytoskeletal regulation and cell morphology.
  • To understand the signaling pathways influenced by EEPD1.

Main Methods:

  • Gene depletion studies (e.g., siRNA or CRISPR) to assess EEPD1 function.
  • Biochemical assays to measure protein activity (e.g., kinase assays).
  • Cell imaging techniques to analyze actin polymerization, lamellipodia formation, and nuclear morphology.

Main Results:

  • EEPD1 promotes actin polymerization, lamellipodia formation, and cell migration.
  • EEPD1's actin-regulatory function is partially dependent on its lipidation.
  • EEPD1 depletion causes abnormal nuclear morphology and affects key signaling proteins (SRC, RAC1, cortactin, profilin).
  • EEPD1 positively regulates SRC kinase activity, crucial for actin polymerization.

Conclusions:

  • EEPD1 is a novel regulator of actin polymerization signaling.
  • EEPD1 links actin dynamics to nuclear morphology and DNA repair processes.
  • EEPD1's functions extend beyond DNA repair, impacting fundamental cellular processes.