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Nho Luong, PhD

Nho Luong, PhD

Assistant Professor

940 Stanton L. Young Blvd., Oklahoma City, OK 73104

405-271-3237

nho-luong@ou.edu

The Luong Laboratory seeks to understanding how post-translational modifications, particularly protein acylation, coordinate stress responses that maintain genome integrity and determine cancer cell fate. Our overarching goal is to define fundamental principles of cellular organization and adaptation that can be leveraged for therapeutic innovation in cancer and age-related diseases.

Academic Section(s):

Oncology Science

Education:

I earned my PhD in Biomedical Sciences at the University of Tsukuba, Japan, under the guidance of Drs. Yoshito Kumagai and Yumi Abiko. My graduate studies focused on how reactive oxygen and sulfur species regulate redox-sensitive signaling and stress adaptation. I then completed postdoctoral training with Dr. Kathryn D. Held (Gunma University; MGH/HMS) and Dr. David Yu (Emory University). My postdoctoral work focused on post-translational mechanisms regulating DNA repair in response to radiotherapy and chemotherapy.

My training was supported by a Japanese Government Scholarship, an Early-Career Scientist Grant from the Japan Society for the Promotion of Science, and an NIH/NIGMS K99/R00 Pathway to Independence Award. I also received sevaral honors, including Young Investigator Awards from the Pharmaceutical Society of Japan, the Asian Society of Toxicology, the Best PhD Dissertation Award from the University of Tsukuba, and Postdoctoral Awards from the American Society for Biochemistry and Molecular Biology and the Radiation Research Society.

Clinical/Research Interests:

I am currently focused on understanding the nuclear roles of reversible lysine myristoylation, a 14-carbon fatty acid modification catalyzed by NMT1/NMT2 and removed by sirtuins and HDACs. Using chemical proteomics, I defined a set of myristoylated proteins enriched for factors that maintain genome stability. Within this set, the repair factor Ku70 emerged as a substrate whose myristoylation responds to DNA damage. This modification is required for Ku70's recruitment to double-strand breaks and for assembly of the repair machinery. Loss of myristoyltransferase activity destabilizes the genome, impairs double-strand break repair, and sensitizes cancer cells to DNA-damaging therapy. These findings establish reversible lysine myristoylation as a regulatory layer of genome maintenance and a therapeutic vulnerability (Luong et al., manuscript in preparation).

Building on these discoveries, my laboratory at the University of Oklahoma integrates chemical biology, quantitative proteomics, genome engineering, and live-cell imaging to define how protein acylation regulates the assembly and function of DNA repair complexes. Current directions include:

  1. Elucidating the roles of reversible lysine myristoylation and other acyl modifications in DNA repair and nuclear organization.
  2. Defining the interplay between protein acylation and redox signaling in cancer cell fate.
  3. Developing genetically encoded acylation-switch technologies to manipulate DDR signaling and therapeutic responses.

The long-term goal of my research program is to define fundamental mechanisms that enable cells to adapt to stress and to translate these insights into new therapeutic strategies for cancer and age-related diseases.

Select Publications:

  1. Haji-Seyed-Javadi R, Koyen AE, Rath SK, Wu B, Madden MZ, Hou Y, Kapoor-Vazirani P, Roshika R, Aiello M, Luong NC, Tseng WC, Sesay F, Kim JS, Tan T, Kim S, Gao B, Song BS, Kenney AM, Connolly EC, Yang L, Xhemalce B, Li X, Switchenko JM, Yang X, Buchwald ZS, Deng X, Miller KM, Yao B, Lan L, Zhao W, Yu DS. HELZ is a RNA-DNA helicase that resolves R loops to facilitate homologous recombination repair. Nature Communication. 2026;17(1). PMID: 42493500.
  2. Sesay F, Zhang H, Kapoor-Vazirani P, Jung AT, Essien ME, Bastien AJ, Luong NC, Liu X, Head PE, Duong DM, Yang X, Buchwald ZS, Deng X, Seyfried NT, Yu DS. MRE11 deacetylation by SIRT2 promotes DNA binding to facilitate DNA end resection and ATM-dependent signaling. The Journal of Clinical Investigation. 2026;136(5). PMID: 41505211.
  3. Luong NC*, Kawamura H, Ikeda H, Roppongi RT, Shibata A, Hu J, Jiang JG, Yu DS, Held KD. ATR signaling controls the bystander responses of human chondrosarcoma cells by promoting RAD51-dependent DNA repair. International Journal of Radiation Biology. 2024;100(5):724–35. PMID: 38442236. (*, corresponding author).
  4. Head PE, Kapoor-Vazirani P, Nagaraju GP, Zhang H, Rath SK, Luong NC, Haji-Seyed-Javadi R, Sesay F, Wang SY, Duong DM, Daddacha W, Minten EV, Song B, Danelia D, Liu X, Li S, Ortlund EA, Seyfried NT, Smalley DM, Wang Y, Deng X, Dynan WS, El-Rayes B, Davis AJ, Yu DS. DNA-PK is Activated by SIRT2 Deacetylation to Promote DNA Double-Strand Break Repair by Non-Homologous End Joining. Nucleic Acids Research. 2023;51(15):7972–87. PMID: 37395399.
  5. Doka E*, Ida T*, Dagnell M*, Abiko Y*, Luong NC*, Balog N, Takata T, Espinosa B, Nishimura A, Cheng Q, Funato Y, Miki H, Fukuto JM, Prigge JR, Schmidt EE, Arner ESJ, Kumagai Y, Akaike T, Nagy P. Control of protein function through oxidation and reduction of persulfidated states. Science Advances. 2020;6(1):eaax8358. PMID: 31911946. (*, co-first authors).
  6. Luong NC, Abiko Y, Shibata T, Uchida K, Warabi E, Suzuki M, Noguchi T, Matsuzawa A, Kumagai Y. Redox cycling of 9,10-phenanthrenequinone activates epidermal growth factor receptor signaling through S-oxidation of protein tyrosine phosphatase 1B. The Journal of Toxicological Sciences. PMID: 32493877.

 

Complete list of published work in my bibliography:

https://www.ncbi.nlm.nih.gov/myncbi/nho.luong.1/bibliography/public/