Nancy S. Bae, Ph.D.

Associate Professor
Glendale, AZ

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Associate Professor

Glendale, AZ

Arizona College of Osteopathic Medicine
Arizona College of Optometry
College of Dental Medicine-Arizona
College of Graduate Studies - AZ
College of Health Sciences - AZ
Arizona College of Podiatric Medicine
College of Veterinary Medicine

Biochemistry and Molecular Genetics

Biomedical Sciences (M.B.S.)
Dental Medicine
Entry into Practice Doctor of Nurse Anesthesia Practice
Post Master's Doctor of Nurse Anesthesia Practice (D.N.A.P.)
Master of Science in Precision Medicine
Nurse Anesthesia Practice (M.S.)
Osteopathic Medicine
Physician Assistant Studies
Podiatric Medicine
Post-Graduate Certificate in Precision Medicine

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University of Maryland | 2003 | Ph.D.
State University of New York at Stony Brook | 0 | M.S.
University of Washington | 0 | B.A.

Courses Taught

BIOCG 1550


BIOCG 1511

BIOCG 1512

BIOCG 1522

BIOCG 1523

BASIG 1501

BASIG 1510



Research summary:

My laboratory research focuses on the functions of the telomere protecting protein RAP1 (also known as TERF2IP). Telomeres are specialized structures found at the ends of linear, eukaryotic chromosomes. They function as a buffer to the progressive loss of DNA that occurs as cells divide, and they prevent the recombination of chromosomes in these repeats and protect chromosomes from end-to-end joining via the recruitment of various proteins.

First identified in the budding yeast Saccharomyces cerevisiae, the Repressor/Activator Protein 1 (RAP1) has been shown to be involved in the activation of expression for many genes. Yeast RAP1 binds to telomeres to help maintain their length and keep the telomeres in a repressive chromatin structure. The human ortholog is part of a six-member protein complex called shelterin. Among the subunits of the complex are TERF1 and TERF2, which bind directly to the telomere repeats. TERF2 recruits the RAP1 protein, and so it has been named TERF2 interacting protein (TERF2IP).

Like the yeast RAP1, the human protein has been found to associate with non-telomeric DNA. Its exact function at these interstitial chromosome sites has not yet been elucidated. Another interesting aspect of the human RAP1 protein is that it has been shown to be in the cytoplasm, most likely leaving the telomeres and translocating out of the nucleus.

Project 1: Roles of cytoplasmic RAP1 and the response to oxidative stress

Project 2: Non-telomeric roles of RAP1 in the nucleus

Project 3: Association of RAP1 and chromatin remodeling factors


  1. Nancy S. Bae, Andrew P. Seberg, Leslie P. Carroll, and Mark J. Swanson. Identification of Genes in Saccharomyces cerevisiae that are Haploinsufficient for Overcoming Amino Acid Starvation. (2017) Genes|Genomes|Genetics. 7(4):1061-1084
  2. Mark J. Swanson, Michelle E. Baribault, Joanna N. Israel and Nancy S. Bae. (2016) Levels of the telomere protein RAP1 are affected by cellular aging and oxidative stress. Biomed Rep. Aug; 5(2):181-187. Epub 2016 Jun 28
  3. Synthesis of a CNS-penetrating FTO inhibitor with anticonvulsant and miRNA modulatory activities.  Guanqun Zhen, Thomas Cox, Leah Tribbey, Gloria Z. Wang, Pauliana Iacoban, Matthew E. Booher, Gregory J. Gabriel, Lu Zhou, Nancy Bae, Joie Rowles, Chuan He, and Mark J. Olsen. (2014) Synthesis of a CNS-penetrating FTO inhibitor with anticonvulsant and miRNA modulatory activities.  ACS Chem Neurosci. 5(8):658-65
  4.  Jay Sarthy, Nancy S. Bae, Jonathan Scrafford, and Peter Baumann. (2009) Human RAP1 Inhibits Non-homologous End-Joining at Telomeres. EMBO J. 2009 Nov 4; 28(21):3390-9. Epub 2009 Sep 17 (Reviewed and featured in EMBO Journal 2009 Nov 4;28(21):3277-3278)
  5. Nancy S. Bae and Peter Baumann. (2007) A Rap1/Trf2 Complex Inhibits Non-Homologous End Joining at Human Telomeric DNA Ends. Mol Cell 2007 May 11; 26(3):323-34 (Reviewed and featured in Mol Cell 2007 26(4):463-4)
  6. Jeremy T. Bunch, Nancy S. Bae, Jessica Leonardi, and Peter Baumann. (2005) Distinct Requirements for Pot1 in Limiting Telomere Length and Maintaining Chromosome Stability. Mol Cell Biol 25(13): 5567-78