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Name: Song Gao
Title: Deputy Director and Professor
Email: gaosong@sysucc.org.cn

Dr. Song Gao is professor of structural biology in SYSUCC. Dr. Gao obtained his Bachelor degree in biotechnology at Wuhan University, 2005. He then went to Europe for graduate study and obtained Master degree in Structural proteomics at University of St Andrews in UK, 2006 and Doctor degree with “Summa Cum Laude” at Max-Delbrück-Centrum for Molecular Medicine (MDC)/Freie Universtät Berlin, Germany, 2011. During his time in Germany, he started to investigate the functional mechanisms of dynamin superfamily. After a short period of postdoc training in MDC, Dr. Gao was granted the National Recruitment Program of Global Youth Experts and moved to SYSUCC to start his own research group in 2012. In SYSUCC, Dr. Gao has established a multi-disciplinary research platform which combines structural biology with single-molecule biophysics, biochemistry and cell biology. Dr. Gao is currently supported by several research grants from the National Natural Science Foundation of China, National Basic Research Program of China, and Natural Science Foundation of Guangdong Province. The research of Dr. Gao’s group is focused on (1) Molecular basis of membrane remodelling mediated by dynamin superfamily, and (2) RNA-manipulating enzymes involved in tumorigenesis and metastasis.


1. Molecular basis of membrane remodelling mediated by dynamin superfamily

Members of the dynamin superfamily catalyze fission and fusion of various   membrane-remodeling proteins that are responsible for many fundamental cellular events in eukaryotes, such as endocytosis, mitochondrial dynamics, and resistance to certain viruses. Malfunction of these proteins causes various human diseases, including neurodegenaration, diabetes and cancer. Dynamin family proteins are multi-domain GTPases which catalyse membrane fission and fusion through orchestrated GTP hydrolysis and self-oligomerization.
    Our group is working on the functional mechanisms of the dynamin superfamily. We use a variety of techniques, including X-ray crystallography, single-molecule biophysics, as well as biochemistry and cell biology methods to investigate how dynamin family members mediate membrane remodeling, and what is the structural difference between the fission- and fusion-related members. Particularly, we focus on the MxA protein which represents the fission dynamins, and mitofusins that are involved in mitochondrial outer membrane fusion.

2. RNA-manipulating enzymes involved in tumorigenesis and metastasis
The development of modern sequencing techniques has helped to reveal various genes or transcripts that are involved in tumorigenesis and metastasis. Some of them encode proteins with undefined biochemical function. In many cases, these proteins show no sequence homology to other known protein families, and are therefore difficult to characterize.
    We start from revealing the structures of these unknown proteins, and aim to find out the hidden kinship between these proteins and other known proteins by their folding pattern. This three-dimensional strategy enables us to accurately define the biochemical function of given known proteins. Of these candidates, we are particularly interested in enzymes involved in RNA manipulation. Up to know, we have identified several novel endoribonucleases and nucleotidyl transferases related to cancer. By systematic functional characterization of these potential drug targets, our research provides important insights that contribute to the development of corresponding approaches against cancer.


2007-2011: PhD at Max-Delbrück-Centrum for Molecular Medicine (MDC)/Freie Universtät Berlin, Germany (with “Summa Cum Laude”).

2005-2006: MRes in Structural Proteomics, School of Biology, University of St Andrews, UK.

2001-2005: BSc in Biotechnology in College of Life Sciences, Wuhan University, P. R. China.


Selected publications:
1. Yu-Lu Cao, Shuxia Meng, Yang Chen, Jian-Xiong Feng, Dong-Dong Gu, Bing Yu, Yu-Jie Li, Jin-Yu Yang, Shuang Liao, David C. Chan, Song Gao. MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion. Nature 2017, 542(7641):372-376

2. Yang Chen, Lei Zhang, Laura Graf, Bing Yu, Yue Liu, Georg Kochs, Yongfang Zhao, Song Gao. Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET. Nature Communications 2017, 8:15744

3. Song Gao, Alexander von der Malsburg, Alexej Dick, Katia Faelber, Gunnar F. Schröder, Otto Haller, Georg Kochs, Oliver Daumke. Structure of myxovirus resistance protein a reveals intra- and intermolecular domain interactions required for the antiviral function. Immunity 2011, 35(4):514-525

4. Katja Faelber, York Posor, Song Gao, Martin Held, Yvette Roske, Dennis Schulze, Volker Haucke, Frank Noé, Oliver Daumke. Crystal structure of nucleotide-free dynamin. Nature 2011, 477(7366):556-560

5. Song Gao, Alexander von der Malsburg, Susann Paeschke, Joachim Behlke, Otto Haller, Georg Kochs, Oliver Daumke. Structural basis of oligomerization in the stalk region of dynamin-like MxA. Nature 2010, 465(7297):502-506

6. Chee Seng Hee#, Song Gao#, Bernhard Loll, Marcia M. Miller, Barbara Uchanska-Ziegler, Oliver Daumke, Andreas Ziegler. Structure of a classical MHC class I molecule that binds "non-classical" ligands. PLoS Biology 2010, 8(12):e1000557

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