βA4-Crystallin Mutations Disrupt Structural Stability and Crystallin Interactions in Congenital Cataract Pathogenesis
The present study revealed mutations in βA4-crystallin-driven cataractogenesis via distinct mechanisms according to their distinct structural contexts. αA-crystallin functions as a primary mitigator of severe misfolding, preferentially stabilizing aggregation-prone conformers. These findings suggest that mutation-specific stabilization via small-molecule chaperones or enhanced αA-crystallin activity may represent potential precision therapeutic strategies for βA4-crystallin-associated congenital cataracts.
Authors
- Ting Jin (ORCID: https://orcid.org/0000-0003-2296-0590)
- Xiaoshan Lin (ORCID: https://orcid.org/0000-0002-8913-5539)
- Shasha Deng
- Muziying Liu (ORCID: https://orcid.org/0000-0002-3084-2431)
- Venkata Pulla Rao Vendra (ORCID: https://orcid.org/0000-0003-0223-9464)
- Zhe Xu (ORCID: https://orcid.org/0000-0002-9705-8924)
- Xulin Zhang
- J. Fielding Hejtmancik
- Qiwei Wang
- Jinyu Yang
- Tinfeng Qin
- Wenqian Li
Institutions
- University of Science and Technology of China (CN)
- Sun Yat-sen University (CN)
- National Eye Institute (US)
- Sun Yat-sen University Cancer Center (CN)
Publication Details
- Journal
- Investigative Ophthalmology & Visual Science
- Published
- 2026-03-13
- DOI
- https://doi.org/10.1167/iovs.67.3.29
- Primary Topic
- Connexins and lens biology
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Natural Science Foundation of China
- Basic and Applied Basic Research Foundation of Guangdong Province