I am eager to join the Life Science and Medicine Forum of the Hong Kong Laureate Forum to engage with leading scientists and fellow young researchers in exploring pressing biomedical challenges. My research centers on the cellular stress response, particularly the Unfolded Protein Response (UPR) and its role in restoring endoplasmic reticulum (ER) homeostasis. I focus on the IRE1 pathway, investigating how its signaling is regulated through oligomeric transitions and attenuated after stress resolution. These mechanisms are fundamental to cell survival and have profound implications in diseases such as neurodegeneration and cancer.

Participating in this forum offers a unique opportunity to exchange ideas across disciplines, gain insights into groundbreaking discoveries, and receive mentorship from esteemed laureates. I am especially drawn to the forum’s commitment to fostering scientific curiosity and collaboration across borders. Engaging in thoughtful dialogue with peers and pioneers will broaden my perspective and inspire innovative directions in my work.

I hope to contribute my enthusiasm for translational research and learn from others who are equally passionate about advancing human health. Being part of this vibrant scientific community would be both an honor and a catalyst for my development as a biomedical scientist.

My research focuses on the cellular stress response and its role in maintaining health or contributing to disease. I aim to understand how cells detect, respond to, and resolve stress at the molecular level. Proper stress response is essential for cellular homeostasis, while its dysregulation is linked to various diseases, including neurodegenerative disorders, metabolic conditions, and cancer.

A central pathway I study is the Unfolded Protein Response (UPR), which monitors protein folding in the endoplasmic reticulum (ER). When misfolded proteins accumulate, the UPR is activated to reduce stress and restore normal function. The UPR comprises three branches—IRE1, PERK, and ATF6—that work together to reestablish ER homeostasis.

My research specifically investigates IRE1, an ER transmembrane sensor and effector. Upon stress, IRE1 oligomerizes from monomers into dimers, tetramers, and higher-order complexes to become active. I focus on two key questions:

1) How is IRE1 signaling attenuated once ER stress is resolved?

2) What are the functional and structural differences between IRE1's oligomeric states?

These studies aim to deepen our understanding of stress regulation at the molecular level and may offer new insights into therapeutic strategies for stress-related diseases.