Biomedical Research Education & Training
Faculty Member

Yang, Elizabeth Ching-Wen, M.D., Ph.D.
Adjunct Associate Professor of Pediatrics

Lab Url: N/A

Phone Number: 615-936-3585

Email Address:

Yang, Elizabeth's picture
Academic history
A.B./M.S., University of Chicago
M.D., Ph.D., Stanford University School of Medicine
Residency, Massachusetts General Hospital
Clinical fellow, St. Louis Children's Hospital
Postdoctoral fellow, Washington University, St. Louis, MO

Office Address   Mailing Address

518 Preston Research Building

397 PRB 6310

Research Keywords
Apoptosis, BCL2 family, BAX and BAK, Cancer,Cell cycle,Phosphorylation,Signal transduction, growth arrest, quiescence, Enzyme action,Phosphatases, Shp2, leukemogenesis, bone marrow reconstitution,Apoptosis,Cancer,Cell cycle,Enzyme action,Kinase,Malignancy,Molecular medicine,Mouse,Phosphorylation,Signal transduction

Clinical Research Keywords
sickle cell disease

Patient Care Specialty
pediatric hematology-oncology

Research Description
We have 3 areas of interest. First is how the BCL2 family of apoptosis molecules regulate cell cycle. We found that the pro-apoptotic BCL2 family members BAX and BAK regulate p27 level and reactive oxygen species, and knockout of BAX and BAK result in quiescence. We are interested in how BAX and BAK deletion decreases intracellular ROS and causes the quiescence phenotype.

Second, the oncogenic protein tyrosine phosphatase Shp2 functions both in apoptosis and proliferation. Mutations of this gene are found in human leukemias. When found in the germline, Shp2 mutations predispose to leukemia. We use retroviral gene transduction and bone marrow reconstitution to study cooperating events in Shp2 murine leukemogenesis.

Third, any apoptotic molecules are regulated by reversible phosphorylation. We identified a PP2A as the enzyme dephosphorylating the transcription factor FOXO1 in response to an apoptotic stimulus through complex competitive interactions with 14-3-3. We are elucidating the regulation of the PP2A phosphatase.

Clinical Research Description
Sickle cell disease is a single gene disease, but with variable clinical severity. We are interested in genetic modifiers of disease expressivity.

Clinical Interests
Sickle Cell disease

Cui, Q, Valentin, M, Janumyan, Y, Yang, E. Bax-/- bak-/- cells exhibit p27 Thr198 phosphorylation and autophagy. Autophagy, 5(2), 263-4, 2009 PMCID:2673855

Prasad, P, Kant, JA, Wills, M, O''Leary, M, Lovvorn, H, Yang, E. Loss of heterozygosity of succinate dehydrogenase B mutation by direct sequencing in synchronous paragangliomas. Cancer Genet Cytogenet, 192(2), 82-5, 2009 PMCID:2810859

Janumyan, Y, Cui, Q, Yan, L, Sansam, CG, Vanlentin, M, Yang, E. G0 function of BCL2 and BCL-xL requires BAX, BAK, and p27 phosphorylation by Mirk, revealing a novel role of BAX and BAK in quiescence regulation. J Biol Chem, 2008 PMCID:2590681

Lavin, VA, Hamid, R, Patterson, J, Alford, C, Ho, R, Yang, E. Use of human androgen receptor gene analysis to aid the diagnosis of JMML in female noonan syndrome patients. Pediatr Blood Cancer, 51(2), 298-302, 2008

Valentin, M, Yang, E. Autophagy is activated, but is not required for the G0 function of BCL-2 or BCL-xL. Cell Cycle, 7(17), 2762-8, 2008

Yan, L, Lavin, VA, Moser, LR, Cui, Q, Kanies, C, Yang, E. PP2A regulates the pro-apoptotic activity of FOXO1. J Biol Chem, 283(12), 7411-20, 2008 PMCID:2276329

Zinkel, S, Gross, A, Yang, E. BCL2 family in DNA damage and cell cycle control. Cell Death Differ, 2006

Cheng N, Janumyan YM, Didion L, Van Hofwegen C, Yang E, Knudson CM. Bcl-2 inhibition of T-cell proliferation is related to prolonged T-cell survival.. Oncogene, 23(21), 3770-3780, 2004

Chiang, Chi-Wu, Kanies, Cindy, Kim, Kwang Woon, Fang, Wei Bin, Parkhurst, Christina, Xie, Minhui, Henry, Travis, Yang, Elizabeth. Protein phosphatase 2A dephosphorylation of phosphoserine 112 plays the gatekeeper role for BAD-mediated apoptosis. Mol Cell Biol, 23(18), 6350-62, 2003 PMCID:193703

Irvin, Brenda J, Wood, Lauren D, Wang, Lilin, Fenrick, Randy, Sansam, Courtney G, Packham, Graham, Kinch, Michael, Yang, Elizabeth, Hiebert, Scott W. TEL, a putative tumor suppressor, induces apoptosis and represses transcription of Bcl-XL. J Biol Chem, 278(47), 46378-86, 2003

Janumyan, Yelena M, Sansam, Courtney G, Chattopadhyay, Anuja, Cheng, Ningli, Soucie, Erinn L, Penn, Linda Z, Andrews, David, Knudson, C Michael, Yang, Elizabeth. Bcl-xL/Bcl-2 coordinately regulates apoptosis, cell cycle arrest and cell cycle entry. EMBO J, 22(20), 5459-70, 2003 PMCID:213787

Greider, Courtney, Chattopadhyay, Anuja, Parkhurst, Christina, Yang, Elizabeth. BCL-x(L) and BCL2 delay Myc-induced cell cycle entry through elevation of p27 and inhibition of G1 cyclin-dependent kinases. Oncogene, 21, 7765-75, 2002

Chattopadhyay, A, Chiang, C W, Yang, E. BAD/BCL-[X(L)] heterodimerization leads to bypass of G0/G1 arrest. Oncogene, 20(33), 4507-18, 2001

Chiang, C W, Harris, G, Ellig, C, Masters, S C, Subramanian, R, Shenolikar, S, Wadzinski, B E, Yang, E. Protein phosphatase 2A activates the proapoptotic function of BAD in interleukin- 3-dependent lymphoid cells by a mechanism requiring 14-3-3 dissociation. Blood, 97(5), 1289-97, 2001

Chen G, Branton PE, Yang E, Korsmeyer SJ, Shore GC. Adenovirus E1B 19 kDa death suppressor protein interacts with BAX but not with BAD. J Biol Chem, 271, 24221-24225, 1996

Yang, E., and Korsmeyer, S.J. Molecular Thanatopsis: a discourse on the BCL2 family and cell death. Blood, 88, 386-401, 1996

Zha, J., Harada, H,, Yang, E., Jockel, J., Korsmeyer, SJ. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-XL. Cell, 87, 619-628, 1996

Domer PH, Head DR, Renganathan N, Raimondi SC, Yang E, Atlas M. Molecular analysis of 13 cases of MLL/11q23 secondary acute leukemia and identification of topoisomerase II consensus-binding sequences near the chromosomal breakpoint of a secondary leukemia with the t(4;11). Leukemia, 9, 1305-1312, 1995

Sedlak, T.W., Oltvai, Z.N., Yang, E., Wang, K., Boise, L.H., Thompson, C.B., Korsmeyer, S.J. Multiple Bcl-2 family members demonstrate selective dimerizations with Bax. PNAS, 92, 7834-7838, 1995

Yang, E., Zha, J., Jockel, J., Korsmeyer. S.J. Bad: a heterodimeric partner of Bcl-xL and Bcl-2, displaces Bax and promotes cell death. Cell, 80, 285-291, 1995

Silverman GA, Yang E, Profitt JH, Zutter M, Korsmeyer SJ. Genetic transfer and expression of reconstructed yeast artificial chromosomes containing normal and translocated Bcl-2 proto-oncogenes. Mol Cell Biol , 13, 5469-5478, 1993

Friedberg EC, Cooper JA, Couto L, Fleer R, Kalainov D, Naumovski L, Nicolet CM, Rehm J, Robinson GW, Ryu BH, Sugino A, Sugino T, Weiss WA, Yang E. Recent Advances in the Characterization of Genes and Proteins for Nucleotide Excision Repair in the Yeast Saccharomyces cerevisiae. Photobiochem Photobiophys Suppl, 333-341, 1987

Friedberg EC, Fleer R, Naumovski L, Nicolet CM, Robinson GR, Weiss WA, Yang E. Nucleotide Excision Repair Genes from Yeast Saccharomyces cerevisiae. In , 231-242, 1986

Yang E, Friedberg EC. The Molecular cloning and nucleotide sequence analysis of the RAD1 gene of Saccharomyces cerevisiae. Mol Cell Biol , 4, 2161, 1984

Friedberg EC, Naumovski L, Yang E, Pure G, Schultz RA, Love JD. Approaching the Biochemistry of Excision Repair in Eukaryotic Cells: The Use of Cloned Genes from Saccharomyces cerevisiae. . In "Cellular Responses to DNA Damage," (EC Friedberg, BA Bridges, eds) Alan R Liss & Co Inc, New York, 62, 1983

Postdoctoral Position Available

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