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| Born Beijing, China, 1971. |
| Peking University, B.S., 1995. |
| Rutgers University, New Brunswick, M.S., 1997. |
| University of California, Berkeley, Ph.D., 2003. |
| Harvard Medical School, Postdoctoral Fellow, 2003-2006. |
| University of Chicago, Assistant Professor 2006-. |
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| Accolades |
| 2006 Camille and Henry Dreyfus New Faculty Award |
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| Jun Yin |
| Assistant Professor |
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| Research Interests |
The research of our lab is at the interface of chemistry, biology and medicine. We are working toward:
- Developing new chemical tools to study biological problems. We are developing new methods for high throughput profiling of cell signaling networks and for molecular imaging of biological processes in the living cell.
- Elucidating the biochemical mechanism of signal transduction mediated by cell surface receptors such as ErbB receptor tyrosine kinases.
- Enzyme engineering for the biosynthesis of structurally diversified natural products with new medicinal activities.
To achieve these goals, our lab develops and employs a wide variety of biochemical and biophysical methods, including DNA library construction, phage display, enzyme directed evolution, organic synthesis, cell culturing, chemical genetics, high throughput proteomics, enzyme kinetics and molecular imaging. |
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| Specific projects in the lab include: |
| 1) Signal transduction mechanisms – global profiling of posttranslational modification enzymes for cell signaling. |
| Communication and coordination of various cellular events from cell division to apoptosis depend on the transduction of dynamic cellular signals encoded by one universal chemical language – protein posttranslational modification (PTM). For example, PTMs such as phosphorylation, glycosylation, methylation, acetylation and lipidation all play central roles mediating signal transduction either by modulating protein – protein interactions or by affecting the subcellular localization of the modified proteins. Two major challenges for mapping the signal transduction networks are: (1) how to identify from the whole proteome the downstream targets of a PTM enzyme such as a kinase or a glycosyltransferase and (2) how to identify from the whole proteome the upstream PTM enzymes that are responsible for a specific modification such as phosphorylation or glycosylation on a signaling molecule. We are thus interested in developing high throughput profiling systems that would allow us to profile the PTM enzymes in the human genome and address those challenges. |
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| 2) Signal transduction mechanisms – detailed mechanistic studies on ErbB receptor signaling by photo crosslinking and molecular imaging. |
| The four members of the ErbB receptor tyrosine kinases play fundamental roles in signal transduction cascades controlling tissue growth in both normal developmental processes and pathological states such as cancer. The binding of various growth factor ligands to the ErbB receptors elicits a complex array of receptor homo and heterodimerization and activates different signaling pathways. Two fundamental questions of the complex signaling events mediated by ErbB receptors are the focus of our lab: (1) do different ligands induce different ErbB receptor dimerization patterns as a way to mediate different signals and (2) do different combinations of ErbB receptor dimerization have different endocytic behaviors as a way for fine-tuning the length and the strength of the mediated signals. To address those questions, ErbB receptors expressed on the cell surface are site specifically labeled with photo crosslinking reagents or fluorescent probes in order to study their interactions with each other and their endocytic pathways. |
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| 3) Enzyme directed evolution – combinatorial biosynthesis of “unnatural” natural products. |
| Polyketides and nonribosomal peptides are two large classes of pharmacologically important natural products as a rich source of anticancer (epothilone, bleomycin) and antibiotic (vancomycin, erythromycin) agents. The biosyntheses of these natural products share the same logic by stepwise chain elongation on multimodular polyketide synthase (PKS) or nonribosomal peptide synthetase (NRPS) as the enzymatic assembly line of simple building blocks – carboxylic acids for PKS and amino acids for NRPS. There has been a great interest for diversifying the structures of polyketides and nonribosomal peptides in order to optimize their biological activities. Unfortunately the structural complexity of these natural products poses a daunting challenge for total synthesis or chemical modification. We are thus trying to reprogram the PKS and NRPS assembly lines by enzyme directed evolution for the biosynthesis of “unnatural” natural products with redesigned structures and desired biological activities. |
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Organic 