TAE‐YOUNG YOONAssociate Professor Department of Biological Sciences Seoul National University Seoul 08826, South Korea E‐mail: [email protected]RESEARCH INTERESTSingle‐Molecule Biophysics: My research group aims to understand molecular mechanisms of “the integral membrane proteins”, which have been largely shunted aside in spite of their biological and practical importance. My group employs an arsenal of single‐molecule techniques to observe both conformational changes and consequential function of the membrane proteins, which allows direct determination of their structure‐function relationship. We recently reported the disassembly mechanism of the SNARE complex by a proteasome system (20S complex), which provides insights into how AAA+ ATPases tightly couple their ATP hydrolysis and unfolding of protein substrates (JACS 2013 and Science 2015). In addition, my research group is pioneering an approach where we apply mechanical tension to the integral membrane proteins while observing their function, which allows determination of the energy landscape governing conformational changes of the membrane proteins (Nat. Comm. 2013, 2014 and Nat. Chem. Biol. 2015). This series of works is being supported by the National Creative Research Initiative Program (창의적연구진흥과제, 단분자시스 템생물학연구단). Development of Tools for Precision Medicine: My research group is also interested in development of new single‐molecule imaging tools. We recently developed single‐molecule version of co‐immunoprecipitation (co‐ IP) analysis (Nat. Comm. 2013, Nat. Prot. 2013). In molecular biology, the co‐IP analysis has been the gold standard of determining protein‐protein interactions (PPIs) for several decades. By adopting single‐molecule fluorescence microscopy as the detection method (instead of SDS PAGE‐gel and western blotting), we have improved the sensitivity and time‐resolution of the co‐IP analysis by five orders of magnitude, respectively. With the extreme sensitivity and quantitativeness of the developed tool, we demonstrate development of PPI biomarkers that allow precision prediction of drug responses of individual tumors, even in cancer types without actionable genomic mutations. Thus, this suggests a path toward “personalized diagnosis of cancers at the PPI level”, which would expand the concept and scope of the targeted cancer therapy. This work is supported by the Samsung Science and Technology Foundation (삼성미래기술육성재단). Updated May 20, 2017
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TY Yoon CV Short version with full publication recordsyoonlab.snu.ac.kr/TY Yoon_CV.pdf2014. 02 –2016.02 KAIST, Associate Professor with tenure ... Invited talk, Frontier in Biological
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Single‐Molecule Biophysics: My research group aims to understand molecular mechanisms of “the integral membrane proteins”, which have been largely shunted aside in spite of their biological and practical importance. My group employs an arsenal of single‐molecule techniques to observe both conformational changes and consequential function of the membrane proteins, which allows direct determination of their structure‐function relationship. We recently reported the disassembly mechanism of the SNARE complex by a proteasome system (20S complex), which provides insights into how AAA+ ATPases tightly couple their ATP hydrolysis and unfolding of protein substrates (JACS 2013 and Science 2015). In addition, my research group is pioneering an approach where we apply mechanical tension to the integral membrane proteins while observing their function, which allows determination of the energy landscape governing conformational changes of the membrane proteins (Nat. Comm. 2013, 2014 and Nat. Chem. Biol. 2015). This series of works
is being supported by the National Creative Research Initiative Program (창의적연구진흥과제, 단분자시스
템생물학 연구단).
Development of Tools for Precision Medicine: My research group is also interested in development of new single‐molecule imaging tools. We recently developed single‐molecule version of co‐immunoprecipitation (co‐IP) analysis (Nat. Comm. 2013, Nat. Prot. 2013). In molecular biology, the co‐IP analysis has been the gold standard of determining protein‐protein interactions (PPIs) for several decades. By adopting single‐molecule fluorescence microscopy as the detection method (instead of SDS PAGE‐gel and western blotting), we have improved the sensitivity and time‐resolution of the co‐IP analysis by five orders of magnitude, respectively. With the extreme sensitivity and quantitativeness of the developed tool, we demonstrate development of PPI biomarkers that allow precision prediction of drug responses of individual tumors, even in cancer types without actionable genomic mutations. Thus, this suggests a path toward “personalized diagnosis of cancers at the PPI level”, which would expand the concept and scope of the targeted cancer therapy. This work is
supported by the Samsung Science and Technology Foundation (삼성미래기술육성재단).
Updated May 20, 2017
PROFESSIONAL EXPERIENCE 2017. 03 – Seoul National University, Associate Professor
Department of Biological Sciences
2016. 03 –2017.02 Yonsei University
Yonsei‐IBS Institute
2014. 02 –2016.02 KAIST, Associate Professor with tenure
Department of Physics
2014. 01 – Samsung Science and Technology Foundation, Principal Investigator
Fundamental Sciences, Physics discipline
2011. 04 – National Creative Research Initiative, Principal Investigator
Ministry of Science, ICT and Future Planning, South Korea
2010. 09 –2014.02 KAIST, Associate Professor
Department of Physics
2007. 10 –2010.08 KAIST, Assistant Professor
Department of Physics and KAIST Institute for the BioCentury
2006. 7 – 2007. 10 Howard Hughes Medical Institute, Research Associate
University of Illinois, Urbana‐Champaign
2005. 7 – 2006. 7 University of Illinois, Urbana‐Champaign, Research Associate
Department of Physics
2004. 9 – 2005. 6 Seoul National University, Research Fellow
Inter‐University Semiconductor Research Center
EDUCATION
2000. 3 – 2004. 8 Seoul National University, Ph.D. in Electrical Engineering
Thesis advisor: Prof. Sin‐Doo Lee
Thesis title: Control of Supramolecular Orderings by Patterned Surface
Microstructures for Liquid Crystal Displays and Artificial Lipid Rafts
1998. 3 – 2000. 2 Seoul National University, M.S. in Electrical Engineering
1994. 3 – 1998. 2 Seoul National University, B.S. in Electrical Engineering
HONORS & AWARDS 30 Young Scientists who will shine the future of South Korea (commemorated with the 30th anniversary of the
Pohang University of Science and Technology) (December 2016)
(포항공대 개교 30주년 기념, 한국을 빛낼 젊은 과학자 30인)
2015 FILA Basic Science Award (awarded by the Korean Academy of Science and Technology) (November 2015)
(제2회 FILA 기초과학상, 한국과학기술한림원)
Blue Ribbon Lecture, Korean Society of Molecular and Cellular Biology (January, 2015)
(한국분자세포생물학회 Blue Ribbon Lecture)
Selected as Principal Investigator of Samsung Science and Technology Foundation (one of two recipients in the
physics discipline), Samsung Science and Technology Foundation (November, 2013)
(삼성미래기술육성재단 연구책임자 선정)
Outstanding lecture award (2012 Fall Semester, Statistical Physics), College of Natural Science
(2012 자연과학대학 우수강의 교원), KAIST (Feb. 2013)
Outstanding research award, College of Natural Science
(2012 자연과학대학 우수연구 교원), KAIST (December, 2012)
2011 100 Outstanding Research Achievements funded by the Korean government
Selected as one of the Top 5 achievements, First placed in the basic science discipline
(16개 범부처 국가연구개발 우수성과 100선, TOP5 선정, 기초연구부문 최우수성과)
2011 50 Outstanding Research Achievements funded by the Ministry of Education and Science of Korea
(교육과학기술부 선정 기초연구 우수성과 50선)
2011 Selected as Principal Investigator of National Creative Research Initiative of Korea (April, 2011)
(2011 창의적 연구진흥과제 선정, 단분자 시스템 생물학 연구단)
Scientist of the Month, January 2011 awarded by the city of Daejeon
(대전광역시 수여 이달의 과학기술인 상, 2011년 1월)
Outstanding academic achievement award, 40th Anniversary of Foundation of KAIST
(KAIST 개교 40주년 기념 학술상) (Feb. 16, 2011)
SELECTED PUBLICATIONS
[1] J.‐K. Ryu, S. J. Kim, S.‐H. Rah, J. I. Kang, H. E. Jung, D. Lee, H.‐K. Lee, J.‐O. Lee, B. S. Park, T.‐Y. Yoon1 & H.
M. Kim1
Reconstruction of LPS Transfer Cascade Reveals Structural Determinants within LBP, CD14, and TLR4‐MD2 for
Efficient LPS Recognition and Transfer
Immunity 46, 38 (2016). 1 Corresponding author
Summary: Lipopolysaccharide (LPS), the major component of the
outer membrane of Gram‐negative bacteria, binds Toll‐like
receptor 4 (TLR4)‐MD2 complex and activates innate immune
responses. To define the sequential molecular interactions
underlying this transfer, we reconstituted in vitro the entire LPS
transfer process from LPS micelles to TLR4‐MD2. Using single‐
molecule approaches, we characterized the dynamic
intermediate complexes for LPS transfer: LBP‐LPS micelles, CD14‐
LBP‐LPS micelle, and CD14‐LPS‐TLR4‐MD2 complex. The
definition of the structural determinants of the LPS transfer
cascade to TLR4 may enable the development of targeted
therapeutics for intervention in LPS‐induced sepsis.
[2] D. Min, R. E. Jefferson, J. U. Bowie1 & T.‐Y. Yoon1
Mapping the energy landscape for second stage folding of a single membrane protein
Nature Chemical Biology 11, 981 (2015). 1 Corresponding author
‐‐ Featured in more than 10 media worldwide including Phys.org, EureaAlert! and Science Daily
In this work, we reported a single‐molecule method that allows folding study of membrane proteins in a lipid
bilayer environment. Our work suggests a moderate thermodynamic stability for an integral membrane
protein, but with a high kinetic energy barrier that imparts rigidity to the structure.
[3] J.‐K. Ryu, D. Min, S.‐H. Rah, S. J. Kim, Y. Park, H. Kim, C. Hyeon, H. M. Kim, R. Jahn1 & T.‐Y. Yoon1
Spring‐loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover
Science 347, 1485 (2015). 1 Corresponding author
‐‐ Featured in more than 30 media worldwide including EurekAlert!, ScienceDaily and PhysOrg
In this work, we reported that NSF disassembles the SNARE complex, the core machinery for membrane
fusion in all eukaryotes, with a spring‐loaded mechanism that exploits a single round of ATP turnover. This
answers a long‐standing question in the membrane trafficking field.
[4] W. Bae, K. Kim1, D. Min, J.‐K. Ryu, C. Hyeon & T.‐Y. Yoon1
Programmed folding of DNA origami structures through single‐molecule force control