Biography
Dr. Zhe Zhang received his B.S. degree in Biotechnology at Shandong University, China in 2008 and Ph.
D. degree in Biochemistry and Molecular Biology at the Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, in 2015. Then he moved to New York (USA) and did his postdoctoral research in Jue Chen’s laboratory at the Rockefeller University from 2015 to 2019. He focused on the functional and structural characterization of Rab GTPases during his graduate work, and during his postdoctoral research, he studied ligand-gated ion channels.
Dr. Zhang’s work on the cystic fibrosis transmembrane conductance regulator (CFTR) has deepened our mechanistic understanding of this anion channel and has enormous potential for helping people suffering from cystic fibrosis.
Dr. Zhang joined the Peking University and PKU-THU Joint Center for Life Sciences (CLS) in July 2019. Now he is working as a Principal Investigator (PI) in the School of Life Sciences to establish the Lab of Membrane Biology and Biophysics.
Education
2008.9-2015.1, Ph.D., Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China
2004.9-2008.6, B.S., School of Life Sciences, Shandong University, Jinan, China
Professional Experience
2019.7-Now, Principal Investigator, PKU-THU Joint Center for Life Sciences (CLS), Beijing, China
2019.7-Now, Principal Investigator, School of Life Sciences, Peking University, Beijing, China
2015.2-2019.6, Postdoctoral Fellow, The Rockefeller University, New York, NY, USA
Honors and Awards
2025 Outstanding Communist Party Member of Peking University
2024 Aegon-Industrial Fund Fellowship Outstanding Young Scholar Award
2023 Excellent Teaching Award
2022 The Boehringer Ingelheim (BI) Young Faculty Research Award
2021 Best Teaching Award
2021 Xueersi Boya Young Fellow
2020 Bayer Investigator
2019 Yifang Investigator
2018 Blavatnik Regional Awards for Young Scientists: Life Sciences Finalist
2018 Tri-Institutional Breakout Prize for Junior Investigators
Teaching
Biochemistry
Membrane proteins constitute about 1/3 of the total proteins in living organisms. Owing to their essential roles in a variety of fundamental biological processes, membrane proteins constitute the vast majority of current drug targets (about 60%). Therefore, scientific research on membrane proteins not only has its biological significance, but also plays an important role in the drug development.Our lab focuses on the mechanistic study of important membrane proteins, especially the disease-related ones, aiming to illustrate their functional mechanisms as well as to guide the downstream drug development. We mainly carry out structural study using single-particle Cryo-EM and X-ray crystallography. In order to thoroughly understand our scientific questions, we also combine biochemical, cell biology, and all the other necessary techniques. Membrane proteins can be mainly divided into four categories according to their different functions: channels, receptors, transporters, and enzymes. Our lab is particularly interested in two classes of them: transporters and receptors. In the short term, we will first focus on the study of solute carrier (SLC) transporter family. SLC transporters are a kind of secondary transporters, and they are the second largest membrane protein family after GPCR (G-protein coupled receptors). Human has more than 400 SLC transporters which are divided into over 50 subfamilies. SLC transporters passively transport their substrates across the cell membrane down their concentration gradients, or they can transport one substrate against its chemical gradient using the energy from transporting another substrate. The substrates for different SLC members vary greatly, ranging from inorganic ions to neurotransmitters, nutrients, and drugs. In the long term, we will also study different families of membrane receptors, including receptor tyrosine kinases (RTKs) and Notch receptors.
At PKU:
-Representative papers
(#Co-first author, *Corresponding author)
(1) Dong Zhou#, Yang Zhang#, Nanhao Chen#, Shitang Huang, Chen Song*, and Zhe Zhang*; Structural basis of G6P/Pi transport and inhibition in SLC37A4 (2025); Nat. Struct. Mol. Biol. Nov 12. (doi: 10.1038/s41594-025-01711-5)
(2) Yang Zhang and Zhe Zhang*; Structural basis of VAChT inhibition by spiroindolines and alkylsulfones (2025); Structure 34: 1-10. (doi: 10.1016/j.str.2025.10.005)
(3) Dong Zhou, Nanhao Chen, Shitang Huang, Chen Song, and Zhe Zhang*; Mechanistic insights into the acetyl-CoA recognition by SLC33A1 (2025); Cell Discov. 11(1): 36. (doi: 10.1038/s41421-025-00793-1)
(4) Yanyi Song#, Shuyi Jian#, Junlin Teng, Pengli Zheng*, and Zhe Zhang*; Structural basis of human VANGL-PRICKLE interaction (2025); Nat. Commun. 16(1): 132. (doi: 10.1038/s41467-024-55396-3)
(5) Balázs Tóth#, Yuefeng Jiang#, Andras Szollosi, Zhe Zhang, and László Csanády*; A conserved mechanism couples cytosolic domain movements to pore gating in the TRPM2 channel (2024); Proc. Natl. Acad. Sci. USA 121(46): e2415548121. (doi: 10.1073/pnas.2415548121)
(6) Yang Zhang#, Fei Dai#, Nanhao Chen#, Dong Zhou, Chia-Hsueh Lee*, Chen Song*, Yixiao Zhang*, and Zhe Zhang*; Structural insights into VAChT neurotransmitter recognition and inhibition (2024); Cell Res. 34(9): 665-668. (doi: 10.1038/s41422-024-00986-5)
(7) Yu Dang#, Tianyi Zhang#, Shabareesh Pidathala#, Guopeng Wang#, Yijie Wang#, Nanhao Chen#, Chen Song, Chia-Hsueh Lee*, and Zhe Zhang*; Substrates and drug recognition mechanisms of SLC19A3 (2024); Cell Res. 34(6): 458–461. (doi: 10.1038/s41422-024-00951-2)
(8) Shabareesh Pidathala#, Shuyun Liao#, Yaxin Dai#, Xiao Li, Changkun Long, Chi-Lun Chang, Zhe Zhang*, and Chia-Hsueh Lee*; Mechanisms of neurotransmitter transport and drug inhibition in human VMAT2 (2023); Nature 623 (7989): 1086–1092. (doi: 10.1038/s41586-023-06727-9)
(9) Fenglian Liu#, Yu Dang#, Lu Li#, Hao Feng#, Jianlin Li, Haowei Wang, Xu Zhang, Zhe Zhang*, Sheng Ye*, Yutao Tian*, and Qingfeng Chen*; Structure and mechanism of a neuropeptide-activated channel in the ENaC/DEG superfamily (2023); Nat. Chem. Biol. 19(10): 1276-1285. (doi: 10.1038/s41589-023-01401-7)
(10) Xue Bai#, Pengyu Sun#, Xinghao Wang#, Changkun Long#, Shuyun Liao#, Song Dang, Shangshang Zhuang, Yongtao Du, Xinyi Zhang, Nan Li, Kangmin He*, and Zhe Zhang*; Structure and dynamics of the EGFR/HER2 heterodimer (2023); Cell Discov. 9(1): 18. (doi: 10.1038/s41421-023-00523-5)
(11) Yu Dang, Dong Zhou, Xiaojuan Du, Hongtu Zhao, Chia-Hsueh Lee, Jing Yang, Yijie Wang, Changdong Qin, Zhenxi Guo, and Zhe Zhang*; Molecular mechanism of substrate recognition by folate transporter SLC19A1 (2022); Cell Discov. 8(1): 141. (doi: 10.1038/s41421-022-00508-w)
(12) Zelin Duan#, Xuezhen Lin#, Lixia Wang#, Qiuxin Zhen, Yuefeng Jiang, Chuxin Chen, Jing Yang, Chia-Hsueh Lee, Yan Qin, Ying Li, Bo Zhao*, Jianchuan Wang*, and Zhe Zhang*; Specificity of TGF-β1 signal designated by LRRC33 and integrin αVβ8 (2022); Nat. Commun. 13(1): 4988. (doi: 10.1038/s41467-022-32655-9)
(13) Zhaohan Lin#, Yinglin Li#, Yuqi Hang#, Changhe Wang, Bing Liu, Jie Li, Lili Yin, Xiaohan Jiang, Xingyu Du, Zhongjun Qiao, Feipeng Zhu, Zhe Zhang*, Quanfeng Zhang*, and Zhuan Zhou*; Tuning the size of large dense-core vesicles and quantal neurotransmitter release via secretogranin II liquid-liquid phase separation (2022); Adv. Sci. e2202263. (doi: 10.1002/advs.202202263)
(14) Yuefeng Jiang, Tingting Liu, Chia-Hsueh Lee, Qing Chang, Jing Yang*, and Zhe Zhang*; The NAD+-mediated self-inhibition mechanism of pro-neurodegenerative SARM1 (2020); Nature 588(7839): 658-663. (doi: 10.1038/s41586-020-2862-z)
-Others
(1) Meijiao Wang#, Wencheng Xia#, Dan Zhao, Zhaoyi Zhai, Rongjing Chen, Xue Bai, Zhe Zhang, Hao Fan, Jian-Ping Zhang*, Cong Liu*, and Fang Jiao*; Amyloid Fibrillation of a Ninjurin-1-Derived α-Helical Peptide: Structural Insights into Conformational Transition (2025); ACS Nano. 19(40): 35977-35991. (doi: 10.1021/acsnano.5c14731)
(2) Jing Wang#, Zhengyang An#, Zhongsheng Wu#, Wei Zhou#, Pengyu Sun, Piyu Wu, Song Dang, Rui Xue, Xue Bai, Yongtao Du, Rongmei Chen, Wenxu Wang, Pei Huang, Sin Man Lam, Youwei Ai, Suling Liu, Guanghou Shui, Zhe Zhang, Zheng Liu, Jianyong Huang, Xiaohong Fang*, and Kangmin He*; Spatial organization of PI3K-PI(3,4,5)P3-AKT signaling by focal adhesions (2024); Mol. Cell 84(22): 4401-4418. (doi.org/10.1016/j.molcel.2024.10.010)
(3) Xuehui Lyu#, Yingzi Cui#, Yinfei Kong#, Min Yang, Hui Shen, Shuyun Liao, Shiyu Li, Chenrui An, Haoyi Wang, Zhe Zhang, Jennie Ong, Yan Li, and Peng Du*; A transient transcriptional activation governs unpolarized-to-polarized morphogenesis during embryo implantation (2024); Mol. Cell 84(14): 2665-2681. (doi: 10.1016/j.molcel.2024.06.005)
(4) Yansong Zhang#, Siyuan Lin#, Jingyu Peng#, Xiaojuan Liang, Qi Yang, Xue Bai, Yajuan Li, Jinhua Li, Wei Dong, Yue Wang, Ying Huang, Yumeng Pei, Jiabao Guo, Wanni Zhao, Zhe Zhang, Min Liu*, and Alan Jian Zhu*; Amelioration of hepatic steatosis by dietary essential amino acid-induced ubiquitination (2022); Mol. Cell 82(8): 1528-1542. (doi: 10.1016/j.molcel.2022.01.021)
(5) Yingdi Wang, Yiming Niu, Zhe Zhang, Kenneth Gable, Sita D Gupta, Niranjanakumari Somashekarappa, Gongshe Han, Hongtu Zhao, Alexander G Myasnikov, Ravi C Kalathur, Teresa M Dunn, and Chia-Hsueh Lee*; Structural insights into the regulation of human serine palmitoyltransferase complexes (2021); Nat. Struct. Mol. Biol. 28(3): 240-248. (doi: 10.1038/s41594-020-00551-9)
Before PKU:
(1) Fangyu Liu#, Zhe Zhang#, Anat Levit, Jesper Levring, Kouki K. Touhara, Brian K. Shoichet, and Jue Chen*; Structural identification of a hotspot on CFTR for potentiation (2019); Science 364(6446): 1184-1188. (doi: 10.1126/science.aaw7611)
(2) Zhe Zhang#, Fangyu Liu#, and Jue Chen*; Molecular structure of the ATP-bound, phosphorylated human CFTR (2018); Proc. Natl. Acad. Sci. USA 115(50): 12757-12762. (doi: 10.1073/pnas.1815287115)
(3) Zhe Zhang#*, Balazs Tóth#, Andras Szollosi, Jue Chen, and Laszló Csanady*; Structure of a TRPM2 channel in complex with Ca2+ explains unique gating regulation (2018); eLife 7: e36409. (doi: 10.7554/eLife.36409)
(4) Zhe Zhang, Fangyu Liu, and Jue Chen*; Conformational changes of CFTR upon phosphorylation and ATP binding (2017); Cell 170(3): 483-491.e8. (doi: 10.1016/j.cell.2017.06.041)
(5) Fangyu Liu#, Zhe Zhang#, Laszló Csanady, David C Gadsby, and Jue Chen*; Molecular structure of the human CFTR ion channel (2017); Cell 169(1): 85-95.e8. (doi: 10.1016/j.cell.2017.02.024)
(6) Zhe Zhang, and Jue Chen*; Atomic structure of the cystic fibrosis transmembrane conductance regulator (2016); Cell 167(6): 1586-1597.e9. (doi: 10.1016/j.cell.2016.11.014)
(7) Zhe Zhang#, ShanshanWang#, Tong Shen, Jiangye Chen, and Jianping Ding*; Crystal structure of the Rab9A-RUTBC2 RBD complex reveals the molecular basis for the binding specificity of Rab9A with RUTBC2 (2014); Structure 22(10): 1408-1422. (doi: 10.1016/j.str.2014.08.005)
(8) Zhe Zhang, Tianlong Zhang, Shanshan Wang, Zhou Gong, Chun Tang, Jiangye Chen, and Jianping Ding*; Molecular mechanism for Rabex-5 GEF activation by Rabaptin-5 (2014); eLife 3: e02687. (doi: 10.7554/eLife.02687)
