Yungping (Jeffrey) Chiang, Ph.D.
- Center for Cancer Research
- National Cancer Institute
- Building 10 - Magnuson CC, Room 4B10
- Bethesda, MD 20892
- 301-496-1376
- chiangj@mail.nih.gov
RESEARCH SUMMARY
One area of Dr. Chiang's research has been focused on studies of Cbl family proteins and their functions in T cell development and activation by using mouse genetic approaches. Three Cbl members have been identified as c-Cbl (Cbl), Cbl-b and Cbl-3 (Cbl-c) in mammalian cells. Cbl proteins consist of multiple functional domains, including an N-terminal tyrosine-kinase binding (TKB) domain, a ring finger (RF), a proline-rich region (PRO), and a C-terminal leucine-zipper/UBA domain. They interact with multiple protein molecules to influence signaling events via their protein-protein interaction domains. Cbl and Cbl-b proteins have been found to be critical factors in negatively mediating TCR signaling, which he is interested in. Dr. Chiang is also interested in the roles of telomeres in cancer and aging biology
Areas of Expertise
1) mouse genetics
Yungping (Jeffrey) Chiang, Ph.D.
Research
One area of Dr. Chiang's research has been focused on studies of Cbl family proteins and their functions in T cell development and activation by using mouse genetic approaches. Three Cbl members have been identified as c-Cbl (Cbl), Cbl-b and Cbl-3 (Cbl-c) in mammalian cells. Cbl proteins consist of multiple functional domains, including an N-terminal tyrosine-kinase binding (TKB) domain, a ring finger (RF), a proline-rich region (PRO), and a C-terminal leucine-zipper/UBA domain. They interact with multiple protein molecules to influence signaling events via their protein-protein interaction domains. Cbl and Cbl-b proteins have been found to be critical factors in negatively mediating TCR signaling, which he is interested in. Dr. Chiang is also interested in the roles of telomeres in cancer and aging biology. Telomeres are structures at the end of eukaryotic chromosomes, consisting of hexanucleotide repeats and associated proteins, which play a critical role in cellular senescence, apoptosis and tumorigenesis. Telomere length is maintained by telomerase and telomere-associated proteins. Telomerase consists of two essential components, telomerase RNA template (TR), which encodes the template for telomere synthesis, and telomerase reverse transcriptase (TERT), the catalytic subunit of telomerase. A number of telomeric associated proteins have been identified, including telomeric repeat binding factors 1 and 2 (TRF1 and TRF2), TRF1-interacting protein 2 (TIN2), tankyrase 1 and 2, protein interacting with NIMA-interacting factor 1 (PINX1), Rap1 and POT1. To understand the mechanism of maintenance of telomere length, Dr. Chiang has generated several mutant mouse lines related to telomerase, telomere-associated proteins with mouse knockout and transgenic technology.
Publications
Exon 1 disruption alters tissue-specific expression of mouse p53 and results in selective development of B cell lymphomas
Cbl enforces Vav1 dependence and a restricted pathway of T cell development
Pharmacologic modulation of serine/threonine phosphorylation highly sensitizes PHEO in a MPC cell and mouse model to conventional chemotherapy
ATM influences the efficiency of TCRß rearrangement, subsequent TCRß-dependent T cell development, and generation of the pre-selection TCRß CDR3 repertoire
Spontaneous transformation of murine epithelial cells requires the early acquisition of specific chromosomal aneuploidies and genomic imbalances
Biography
Yungping (Jeffrey) Chiang, Ph.D.
In 1996, Dr. Chiang came to National Institute of Allergy and Infectious Diseases as a postdoctoral fellow after he completed his Ph.D. degree in Biochemistry and Molecular Biology in University of Nebraska Medical Center. He joined the laboratory of Dr. Hodes of National Cancer Institute as an IRTA fellow in 1999, and became as a staff scientist in 2004. With gene targeting technology, Dr. Chiang has generated several mouse models for studying the development and activation of T cells, and the biology of telomeres.