Evidence map›Paper›PMID 40589157›Full record

ArticleBiology of the cell2025

The DNA Repair Component EEPD1 Regulates Actin Polymerization.

Robert Hromas, Austin Kirby, Andrew Carrillo, Aruna Jasiwal, Kimi Kong, Manh Tien Tran, Dominic Arris, Elizabeth A Williamson

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biology of the cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Robert HromasDivision of Hematology and Medical Oncology, Department of Medicine and the Mays Cancer Center, University of Texas Health Science Center, San Antonio, Texas, USA.
Austin KirbyDivision of Hematology and Medical Oncology, Department of Medicine and the Mays Cancer Center, University of Texas Health Science Center, San Antonio, Texas, USA.
Andrew CarrilloDivision of Hematology and Medical Oncology, Department of Medicine and the Mays Cancer Center, University of Texas Health Science Center, San Antonio, Texas, USA.
Aruna JasiwalDivision of Hematology and Medical Oncology, Department of Medicine and the Mays Cancer Center, University of Texas Health Science Center, San Antonio, Texas, USA.
Kimi KongDivision of Hematology and Medical Oncology, Department of Medicine and the Mays Cancer Center, University of Texas Health Science Center, San Antonio, Texas, USA.
Manh Tien TranDivision of Hematology and Medical Oncology, Department of Medicine and the Mays Cancer Center, University of Texas Health Science Center, San Antonio, Texas, USA.
Dominic ArrisDivision of Hematology and Medical Oncology, Department of Medicine and the Mays Cancer Center, University of Texas Health Science Center, San Antonio, Texas, USA.
Elizabeth A WilliamsonDivision of Hematology and Medical Oncology, Department of Medicine and the Mays Cancer Center, University of Texas Health Science Center, San Antonio, Texas, USA.

Funding

EEPD1 Repair of Stressed Replication ForksR01CA205224 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Robert A Hromas · 2016 to 2026
$3.3M
EPIGENETIC CONTROL OF NHEJ DNA REPAIRR01CA139429 · NCI · UNIVERSITY OF NEW MEXICO · PI HROMAS, ROBERT A · 2010 to 2014
$1.5M
Biomarkers For BRCA1-Deficient CancersR01CA279971 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Kimi Y Kong · 2024 to 2026
$1.3M
Cancer Prevention and Research Institute of Texas RP220269NCI NIH HHS R01 CA139429NCI NIH HHS R01 CA205224NCI NIH HHS R01 CA279971NIH HHS R01 CA139429
6 · The paper itself

Abstract

Endonuclease exonuclease phosphatase domain-containing protein 1 (EEPD1) is a DNase1 superfamily member that has DNA endonuclease activity. It plays a critical role in multiple DNA repair processes such as oxidative damage repair and stressed replication fork repair. Interestingly, EEPD1 is myristoylated and palmitoylated near its amino terminus in response to high levels of cholesterol, and this localizes EEPD1 protein to the inner cell membrane. Surprisingly, we found that EEPD1 promotes cortical branching actin polymerization and proper lamellipodia formation and is necessary for subsequent cell migration. EEPD1's enhancement of actin polymerization partially required its myristoylation and palmitoylation. EEPD1 depletion also resulted in marked abnormalities in nuclear morphology. Loss of EEPD1 resulted in loss of phosphorylation of SRC, RAC1, cortactin, and profilin, which are essential steps in signaling for actin polymerization. Loss of EEPD1 lowered SRC kinase activity, which would harm actin polymerization. In summary, EEPD1 is a novel, positive regulator of the signaling pathway for actin polymerization, linking actin regulation to nuclear morphology and DNA repair.

Indexed as

ActinsDNA RepairAnimalsCell MovementCortactinHeLa CellsHumansPhosphoprotein PhosphatasesPhosphorylationPolymerizationProfilinsPseudopodiarac1 GTP-Binding ProteinSignal Transductionsrc-Family KinasesActinsCortactinPhosphoprotein PhosphatasesProfilinsrac1 GTP-Binding Proteinsrc-Family KinasesSSH1 protein, humanactincell membranecell migrationEEPD1

Identifiers

PMID40589157
PMCPMC12209743

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.