ICKSMCB 2019 / 2019 International Conference of the Korean Society for Molecular and Cellular Biology / September 17(Mon)-19(Wed), 2019 / COEX, Seoul, Korea

Plenary Lectures

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Plenary Lecture Ⅰ September 30 (Mon), 13:20-14:10, Rm. 401


To Fold or not To Fold: the Yin and Yang of Chaperone-Mediated Client Activation

David. A. Agard, Ph.D.
University of California, San Francisco, USA
Organizer: Byoung Heon Kang, Ph.D. (Ulsan National Institute of Science and Technology (UNIST), Korea)
Chair: Byung-Ha Oh, Ph.D. (Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Korea)

Professor David Agard. A US biophysicist, David joined the faculty of the department of Biochemistry and Biophysics at the University of California, San Francisco in 1983. He is currently a Professor of Biochemistry & Biophysics, Professor of Pharmaceutical Chemistry, and an Investigator with the Howard Hughes Medical Institute. David was the founding Director of the California Institute for Bioengineering, Biotechnology and Quantitative Biomedical Research in 2001, and was its UCSF Scientific Director from 2002-2006. He received his BS in Molecular Biophysics & Biochemistry from Yale in 1975 working with Fred Richards, and PhD in Biological Chemistry from the California Institute of Technology in 1980 working with Robert Stroud. This was followed by a brief postdoc with John Sedat at UCSF and his main postdoctoral work at the MRC Laboratory of Molecular Biology in Cambridge, England with Richard Henderson. Having a strong background in structural biophysics, David's current work focuses on elucidating the mechanisms of assisted folding by the Hsp90 molecular chaperone system and the mechanism of microtubule nucleation. David has been instrumental in the development of direct phasing methods for SAXS, three dimensional deconvolution and Structured Illumination light microscopies, automated cryo-electron tomography, the K2 Summit single electron counting direct detector, and second-generation beam-induced motion correction software. His work has been recognized by his election to the National Academy of Sciences in 2007 and American Academy of Arts and Sciences in 2009. Beyond numerous advisory boards, David served on the National Advisory General Medical Sciences Council at the NIH.

Plenary Lecture Ⅱ September 30 (Mon), 16:40-17:30, Rm. 401

David J. Anderson, Ph.D.

Toward the Mysteries of Sleep

Masashi Yanagisawa, M.D., Ph.D.
University of Tsukuba, JAPAN
Organizer & Chair: Kyungjin Kim, Ph.D. (Deagu Gyeongbuk Institute of Science & Technology (DGIST), Korea)

In 1988, as a graduate student at University of Tsukuba, Yanagisawa discovered endothelin, a potent vasoconstrictor peptide from vascular endothelial cells, which sparked an intense research activity in the field; his original paper has been cited more than 13,000 times by now. In the subsequent year, his group identified a receptor for endothelin, which would become an important drug target; the endothelin receptor antagonist bosentan was approved in 2001 for the treatment of pulmonary hypertension.
He was recruited to University of Texas Southwestern Medical Center at Dallas in 1991 as an HHMI Investigator. In 1996, he initiated a systematic search for endogenous ligands of "orphan" G protein-coupled receptors, which resulted in his 1998 discovery of orexin, a hypothalamic neuropeptide. He then discovered in 1999 that orexin deficiency causes the sleep disorder narcolepsy. This opened up a new avenue in sleep research, leading to better understanding of sleep/wake switching circuitry in the brain. The notion that orexin is an important endogenous waking agent led to the development of orexin receptor antagonists as sleep-inducing drug, first of which, suvorexant, was approved in 2014.
Recognizing, however, that the fundamental mechanism for sleep homeostasis still remains a mystery, in 2010 he embarked upon a highly ambitious project of polysomnography (EEG/EMG)-based forward genetic screen for sleep/wake abnormalities in chemically mutagenized mouse cohort. This large-scale project is now continuing at the International Institute for Integrative Sleep Medicine (WPI-IIIS) in Tsukuba, Japan, and has recently led to identification of several new genes that are importantly involved in the regulation of sleep amounts and the level of sleep need.

Nobel Laureate Lecture I October 1 (Tue), 11:30-12:20, Rm. 401

Looking Back on My 30 years' of Yeast Autophagy Research

Yoshinori Ohsumi, M.D., Ph.D.
Institute of Innovative Research, Tokyo Institute of Technology, JAPAN
*2016 Nobel Laureate
Organizer & Chair: Yong-Keun Jung, Ph.D. (Seoul National University, Korea)

Dr. Yoshinori Ohsumi was born in Fukuoka in 1945. In 1963, he entered to The Univ. of Tokyo. Since he met Prof. K. Imahori, he chose molecular biology as the path of his future. As a graduate student, Dr. Ohsumi studied E. coli ribosome and then colicin E3. Near the end of 1974, he enrolled in Rockefeller Univ., to study under Dr. G. M. Edelman. He returned to Japan at the end of 1977, and worked as an assistant professor under Prof. Y. Anraku at The Univ. of Tokyo. Dr. Ohsumi decided to take up the study of the yeast vacuolar membrane. He succeeded to show active transport systems and a novel proton-pump, v-type ATPase on the vacuolar membrane. In 1988, Dr. Ohsumi moved to College of Arts and Sciences of the same University as an associate prof., and opened up his own small lab. He started to work on the lytic function of the vacuole, then found yeast autophagy by light and electron microscopy. He performed a genetic screen for autophagy-defective mutants. His group got 18 genes essential for starvation-induced autophagy. Then he moved to The National Inst. for Basic Biology at Okazaki, and uncovered that these Atg proteins consist of several functional groups including two ubiquitin-like conjugation systems. His colleagues started studies on ATG homologues in mammals and plant, proving that the ATG system is well conserved in higher eukaryotes. However, up to now, Dr. Ohsumi has focused on dissection of the mechanism of the Atg proteins in yeast at a molecular level. In 2009, he moved to Tokyo Inst. of Tech. and received the Nobel Prize in Physiology or Medicine for the elucidation of mechanisms for autophagy. He continues to elucidate the membrane dynamics and the physiological relevance of autophagy in the same university.
In addition to the research, he established the Ohsumi Frontier Science Foundation in 2016 for the development of basic science and he is working hard to the development of the basic science.

Nobel Laureate Lecture II October 1 (Tue), 15:00-15:50, Rm. 401

Douglas E. Soltis, Ph.D.

The Century of Vision: Protein Structures in Basic Science and Pharma Research

Robert Huber, Ph.D.
Max Planck Institute of Biochemistry, Germany
*1988 Nobel Laureate
Organizer: Hyun Kyu Song, Ph.D. (Korea University, Korea)
Jeong-Sun Kim, Ph.D. (Chonnam National University, Korea)
Chair: Chin Ha Chung, Ph.D. (Seoul National University, Korea)

Robert Huber was born in 1937 in Munich. He studied chemistry at the Technische Universitat Munchen (TUM), where he also completed his Ph.D. and habilitation. Since 1972, he has been a member of the Max-Planck-Gesellschaft and Director at the Max-Planck-Institut fur Biochemie until his retirement in 2005. Since 1976, he also serves at the TUM as a Professor. He holds appointments as Guest Professor at the Universitat Duisburg-Essen (Germany), the Cardiff University (Great Britain), the Universidad Autonoma de Barcelona (Spain), and the Seoul National University (Korea). He serves as a member of the Board and/or Scientific Advisory Board of a number of pharmaceutical and crop science companies, and he is co-founder of two companies, Proteros and Suppremol, located in Martinsried and offering services for drug discovery and development and for the development of novel therapies for autoimmune diseases, respectively. Huber has made major contributions to the understanding of the structure and function of biological macromolecules. He has studied proteases and their natural and synthetic inhibitors, metalloenzymes (iron, nickel, molybdenum, copper), proteins of the immune system (antibodies and antibody receptors), protein hormones and their receptors, protein kinases, enzymes of amino acid biosynthesis, enzymes of cofactor and vitamin biosynthesis and proteins of energy and electron transfer. In addition, he has contributed to the development of instruments for data collection and to methods in protein crystallography, particularly Patterson methods, graphic methods, and refinement, to the use of electron rich metal clusters, and most recently to the methods and instruments for crystal improvement. He has been honoured by numerous honorary doctorates, professorships, memberships in learned societies and awards, including the Otto-Warburg Medal, the Emil von Behring Medal, the Sir Hans Krebs Medal, the The Linus Pauling Medal, Max Tishler Prize and, in 1988, the Nobel Prize for Chemistry together with H. Michel and J. Deisenhofer.

Plenary Lecture Ⅲ October 2 (Wed), 11:30-12:20, Rm. 401

Douglas E. Soltis, Ph.D.

Leveraging Brain Rhythms as a Therapeutic Intervention for Alzheimer's Disease

Li-Huei Tsai, Ph.D.
Massachusetts Institute of Technology, USA
Organizer: Sang Ki Park, Ph.D. (Pohang University of Science and Technology (POSTECH), Korea)
Jinsoo Seo, Ph.D. (Deagu Gyeongbuk Institute of Science & Technology (DGIST), Korea)
Chair: Bong-Kiun Kaang, Ph.D. (Seoul National University, Korea)

Li-Huei Tsai is the Director of the Picower Institute for Learning and Memory at the Massachusetts Institute of Technology, a Picower Professor of Neuroscience, and an Associate Member of the Broad Institute. Tsai is a fellow of the American Association for the Advancement of Science, a member of the National Academy of Medicine, and an Academician of the Academia Sinica in Taiwan.
Tsai is interested in elucidating the pathogenic mechanisms underlying neurological disorders that impact learning and memory. She is a recipient of the Mika Salpeter Lifetime Achievement Award, and the 2018 Hans Wigzell Research Foundation Science Prize for her research on Alzheimer's disease.