The Human Frontier Science Program (HFSP) has released the fourth edition of its HFSP Science Digest, a 60-page compendium highlighting the creativity and global reach of HFSP-supported frontier research. Featuring the work of 89 scientists, including 19 HFSP Fellows and 70 members of HFSP Research Grant teams, research in this year's edition looks at life across many scales, from the smallest molecular assemblies to the vast complexity of ocean ecosystems.

Programmed cell death (PCD) plays a central role in the development of multiple systemic diseases. In a recent review, researchers from China examined how Z-DNA binding protein 1 (ZBP1) regulates PCD and influences disease progression. They summarized the molecular mechanisms controlling ZBP1-mediated cell death, discussed interacting molecules and signaling pathways, and highlighted the potential of targeting ZBP1 as a therapeutic strategy for treating related pathological conditions.

New study led by researchers at Cincinnati Children’s proposes a way to combine previously separate data gathering approaches and concepts about blood cell formation into a more unified whole

This study reports the first in plant synthesis of luminescent and photo-responsive lignin by genetically engineering poplar trees to incorporate scopoletin into the lignin polymer. Through controlled enzyme expression, we achieved lignin with strong, stable luminescence, visible-range emission, and resistance to quenching. Additionally, the material exhibits pH-responsive fluorescence and reversible photo-dimerization, enabling light-controlled functionality. These unique properties open new opportunities for sustainable biomaterials with potential applications in environmental sensing, smart polymers, and advanced photonic materials.

The secretory pathway in eukaryotic cells is crucial for maintaining cellular function and physiological activities, as it ensures the accurate transport of proteins to specific subcellular locations or for secretion outside the cell. A research team led by Prof. GUO Yusong from the Division of Life Science at The Hong Kong University of Science and Technology (HKUST) has been extensively investigating the molecular mechanisms by which cargo proteins are recognized and loaded into transport vesicles in the secretory pathway. The team has successfully reconstituted the packaging of multiple disease-related cargo proteins into vesicles along the secretory route, providing a powerful tool for dissecting the molecular mechanisms of cargo loading. In addition, they developed an innovative analysis platform that integrates vesicle reconstitution with electron microscopy and proteomics, enabling systematic identification of vesicle protein composition and morphological features. This comprehensive approach has proven effective in uncovering novel cargo clients and cellular factors that mediate vesicular trafficking (Figure 1).