2005.09 - 2009.07 Sichuan University, B.S. (Biological Sciences)

2009.09 - 2015.01 Tsinghua University, Ph.D. (Biochemistry and Molecular Biology)

2015.05 - 2020.02 Max Planck Institute of Molecular Cell Biology and Genetics (MPI-CBG), Postdoctoral Researcher

2020.03 - 2021.12 Whitehead Institute, Postdoctoral Researcher

2022.01 - 2025.12 Max Planck Institute of Molecular Cell Biology and Genetics (MPI-CBG), Postdoctoral Researcher

2026.01 - Present Institute of Biophysics, Chinese Academy of Sciences, Principal Investigator

In cells, many essential structures are not “built once and fixed.” Instead, proteins and nucleic acids continuously assemble and disassemble through numerous reversible, transient weak interactions. Liquid-like biomolecular condensates are a classic example: they often form rapidly via weak-interaction–driven phase separation and dissolve just as quickly when no longer needed. Because these interactions are weak, fast-changing, and highly state-dependent, many conventional approaches—well suited for stable structures—struggle to capture the key molecular mechanisms of such processes in their native cellular context.

We aim to understand how protein sequence and structure jointly encode dynamic assembly, what cellular tasks these assemblies enable, and under what conditions they become dysregulated—especially in cancer. We refer to the rule set by which amino acids specify weak interactions and thereby determine dynamic assembly behavior as molecular grammar. Like the genetic codon table, this grammar should be readable: given sequence and structural cues, we want to infer whether a protein can assemble dynamically, how long assemblies persist, and which partners it tends to co-assemble with.

To achieve this, we use high-throughput mutagenesis and quantitative microscopy as a discovery engine. Starting from individual proteins, we systematically perturb key positions and track the emergence and dissolution of assemblies to decode their molecular grammar. We then combine bioinformatics to generalize these principles across related proteins and extract reusable, predictive rules. Finally, we integrate protein biochemistry and cell-based assays to test how changes in assembly translate into specific cellular functions and disease-relevant phenotypes.

Scientific Questions

How do protein sequence and structure encode dynamic assembly (e.g., biomolecular condensates) to control functional outputs?

What essential cellular functions are enabled by dynamic assembly?

When dynamic assembly goes awry, how does it rewire cellular function and drive diseases such as cancer?

What is the “molecular grammar” underlying weak-interaction–driven dynamic assembly?

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(From Jie Wang, January 27, 2026)