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.
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
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
Blavatnik Regional Awards for Young Scientists: Life Sciences Finalist, 2018
Tri-Institutional Breakout Prize for Junior Investigators, 2018
Charles H. Revson Senior Fellowship in Biomedical Science, 2017-2019
China National Scholarship, 2014
Chinese Academy of Sciences Merit Student, 2014
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, about 60% of approved drugs target the membrane proteins. 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.
Representative Peer-Reviewed Publications
1. Fangyu Liu*, Zhe Zhang*, Anat Levit, Jesper Levring, Kouki K. Touhara, Brian K. Shoichet, and Jue Chen$; Structural identification of a hotspot on CFTR for potentiation; Science; 2019,364(6446): 1184-1188. (doi: 10.1126/science.aaw7611) (*co-first author)
2. Zhe Zhang*, Fangyu Liu*, and Jue Chen$; Molecular structure of the ATP-bound, phosphorylated human CFTR; Proc. Natl. Acad. Sci. USA; 2018, 115(50): 12757-12762. (doi: 10.1073/pnas.1815287115) (*co-first author)
3. Zhe Zhang* $, Bal a´zs Tóth*, Andras Szollosi, Jue Chen, and L a´szló Csan a´dy$; Structure of a TRPM2 channel in complex with Ca2+ explains unique gating regulation; eLife; 2018, 7: e36409. (doi: 10.7554/eLife.36409) (*co-first author, $ corresponding author)
4. Zhe Zhang, Fangyu Liu, and Jue Chen$; Conformational changes of CFTR upon phosphorylation and ATP binding; Cell; 2017, 170(3): 483-491.e8. (doi: 10.1016/j.cell.2017.06.041)
5. Fangyu Liu*, Zhe Zhang*, L a´szló Csan a´dy, David C Gadsby, and Jue Chen$; Molecular structure of the human CFTR ion channel; Cell; 2017, 169(1): 85-95.e8. (doi: 10.1016/j.cell.2017.02.024) (*co-first author)
6. Zhe Zhang, and Jue Chen$; Atomic structure of the cystic fibrosis transmembrane conductance regulator; Cell; 2016, 167(6): 1586-1597.e9. (doi: 10.1016/j.cell.2016.11.014)
7. Zhe Zhang*, ShanshanWang*, Tong Shen, Jiangye Chen, and Jianping Ding$; Crystal structure of the Rab9A-RUTBC2 RBD complex reveals the molecular basis for the binding specificity of Rab9A with RUTBC2; Structure; 2014, 22 (10): 1408-1422. (doi: 10.1016/j.str.2014.08.005) (*co-first author)
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; eLife; 2014, 3: e02687. (doi: 10.7554/eLife.02687)