Structural insights into the gating mechanism of the fission yeast phosphate exporter SpXpr1
occluding the exit. We further showed that InsP6 binding induces allosteric destabilization of the N-loop gate, facilitating phosphate release. Functional validation through phosphate efflux assays in Homo sapiens XPR1 (HsXPR1)-knockout cells and whole-cell patch-clamp recordings confirmed the structural observations. Our findings elucidated a unique gating mechanism of SpXpr1 and offer evolutionary perspectives on phosphate regulation across eukaryotes.
Authors
- Huaizong Shen (ORCID: https://orcid.org/0000-0002-1216-5393)
- Chenxi Yue
- Yuxing Wang (ORCID: https://orcid.org/0000-0003-3079-5572)
- Yuechan Wang
- Ye Yu
- Xinran Li
- Hui Yang
Institutions
- China Pharmaceutical University (CN)
- Westlake University (CN)
- Zhejiang University (CN)
Publication Details
- Journal
- Cell Discovery
- Published
- 2026-04-15
- DOI
- https://doi.org/10.1038/s41421-026-00883-8
- Primary Topic
- Plant nutrient uptake and metabolism
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Westlake University
- Ministry of Science and Technology of the People's Republic of China
- Natural Science Foundation of Zhejiang Province