CIMR-Hanjie Jiang

Research Group

Hanjie Jiang

hjiang(at)cimrbj.ac.cn

Lab Website

Assistant Investigator

hjiang(at)cimrbj.ac.cn

Lab Website

B.S. in Pharmaceutical Sciences, Peking University, China

M.S. in Pharmacology, Peking University, China

Ph.D. in Pharmacology and Molecular Sciences, Johns Hopkins University, USA

Work Experience

2025.2-Present

Assistant Investigator, Chinese Institutes for Medical Research, Beijing, China

2022.2-2025.2

Postdoctoral Fellow, Harvard Medical School and Brigham and Women’s Hospital, USA

Research Direction

The Jiang laboratory at CIMR is dedicated to using chemical biology approaches to decode the functions of protein post-translational modifications (PTMs) in cancer and other diseases, with a focus on advancing innovative therapeutic strategies.

Major Research Projects

1. Developing and applying chemical methods, such as protein semisynthesis and molecular probes, to investigate protein ubiquitination, phosphorylation, and other PTMs in key enzyme and cellular signaling pathways.

2. Exploring the regulatory mechanisms of ubiquitin and ubiquitin-like modifications and their pathological roles in disease progression to identify novel therapeutic targets.

3. Designing and optimizing synthetic biology tools for targeted ubiquitination to provide innovative methods for basic research and translational medicine.

Major Contributions

1. Discovered the catalytic role of terminal carboxylate involvement in ubiquitin transfer by HECT E3 ligases (Nature Chemistry, 2024).

2. Uncovered the autoinhibition and activation mechanisms in HECT E3 ligases (Molecular Cell, 2017; JBC, 2019; JBC, 2022).

3. Developed a specific protein N-terminal labeling method (JACS, 2018; Methods in Enzymology, 2020; Current Protocols, 2021).

Representative Publications *：Co-first author; #：Co-corresponding author

Xie G, Gao L, Lu R, Tian L, Zheng T, Li X, Dang Y, Cole PA, Yu X^#, Jiang H^#, Chen Z^#. Biochemical Analysis of PD-L1 ubiquitination by CRL3SPOP, ARIH1, and NEDD4 family ubiquitin ligases. Structure, 2025, 33(8): 1304-1313. DOI: 10.1016/j.str.2025.05.005

Jiang H, Miller BD, Viennet T, Kim H, Lee K, Athanari H, Cole PA. Protein Semisynthesis Reveals Plasticity in HECT E3 Ubiquitin Ligase Mechanisms. Nature Chemistry, 2024, 16: 1894-1905. DOI: 10.1038/s41557-024-01576-z

Jiang H, Chiang CY, Chen Z, Nathan S, D’Agostino G, Paulo JA, Song G, Zhu H, Gabelli SB, Cole PA. Enzymatic analysis of WWP2 E3 ubiquitin ligase using protein microarrays identifies autophagy-related substrates. Journal of Biological Chemistry, 2022, 298: 101854. DOI: 10.1016/j.jbc.2022.101854

Jiang H, Thomas SN, Chen Z, Chiang CY, Cole PA. Comparative analysis of the catalytic regulation of NEDD4-1 and WWP2 ubiquitin ligases. Journal of Biological Chemistry, 2019, 294: 17421-17436. DOI: 10.1074/jbc.RA119.009211

Chen Z, Jiang H, Xu W, Li X, Dempsey DR, Zhang X, Devreotes P, Wolberger C, Amzel LM, Gabelli SB^#, Cole PA^#. A tunable brake for HECT ubiquitin ligases. Molecular Cell, 2017, 66: 345-357. DOI: 10.1016/j.molcel.2017.03.020

Jiang H, Dempsey DR, Cole PA. Ubiquitin ligase activities of WWP1 germline variants K740N and N745S. Biochemistry, 2021, 60: 357-364. DOI: 10.1021/acs.biochem.0c00869

Dempsey DR, Jiang H, Kalin JH, Chen Z, Cole PA. Site-specific protein labeling with N-hydroxysuccinimide-esters and the analysis of ubiquitin ligase mechanisms. Journal of the American Chemical Society, 2018, 140: 9374-9378. DOI: 10.1021/jacs.8b05098

Jiang H, D'Agostino GD, Cole PA, Dempsey DR. Selective protein N-terminal labeling with N-hydroxysuccinimide esters. Methods in Enzymology, 2020, 639: 333-353. DOI: 10.1016/bs.mie.2020.04.018

Jiang H, Cole PA. N‐Terminal Protein Labeling with N‐Hydroxysuccinimide Esters and Microscale Thermophoresis Measurements of Protein‐Protein Interactions Using Labeled Protein. Current Protocols, 2021, 1: e14. DOI: 10.1002/cpz1.14

Lee K^*, Barone M^*, Waterbury AL, Jiang H, Nam E, DuBois-Coyne SE, Whedon SD, Wang ZA, Caroli J, Neal K, Ibeabuchi B, Dhoondia Z, Kuroda MI, Liau BB, Beck S^#, Mattevi A^#, Cole PA^#. Uncoupling histone modification crosstalk by engineering lysine demethylase LSD1. Nature Chemical Biology, 2024. DOI: 10.1038/s41589-024-01671-9

Full List of Publications Can Be Found here