This study identifies six distinct Rab-binding sites on LRRK2 and a GABARAP-binding site, revealing molecular mechanisms of Rab recognition and potential therapeutic targets for Parkinson's disease.

bioRxiv · May 5, 2026 · PreprintBiochemistry

Mechanisms of KCNQ1 gating modulation by KCNE1/3 for cell-specific function

Chenxi Cui, Lu Zhao, Ali A. Kermani, Shuzong Du, Tanadet Pipatpolkai, Meiqin Jiang, Sagar Chittori, Yong Zi Tan, Jingyi Shi, Lucie Delemotte, Jianmin Cui, Ji Sun

This study investigates how KCNE1 and KCNE3 modulate KCNQ1 gating through PIP2-dependent mechanisms, revealing distinct roles in voltage sensitivity and GPCR regulation across cell types.

Cell Research · Jul 31, 2025Peer-reviewedBiochemistry

RAB12-LRRK2 Complex Suppresses Primary Ciliogenesis and Regulates Centrosome Homeostasis in Astrocytes

Xingjian Li, Hanwen Zhu, Bik Tzu Huang, Xianting Li, Heesoo Kim, Haiyan Tan, Yuanxi Zhang, Insup Choi, Junmin Peng, Pingyi Xu, Ji Sun, Zhenyu Yue

This study identifies RAB12 as a LRRK2 substrate in mouse brains, shows its role in suppressing ciliogenesis and regulating centrosome homeostasis in astrocytes, and demonstrates that disrupting RAB12 mitigates PD-linked LRRK2 mutation effects.

Nature Communications · Sep 29, 2024Peer-reviewedNeuroscience