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Structural insights into the mechanism of phosphate recognition and transport by XPR1

文献类型： 外文期刊

作者： Zhang, Wenhui 1 ; Chen, Yanke 1 ; Guan, Zeyuan 1 ; Wang, Yong 2 ; Tang, Meng 1 ; Du, Zhangmeng 1 ; Zhang, Jie 1 ; Cheng, Meng 1 ; Zuo, Jiaqi 1 ; Liu, Yan 1 ; Wang, Qiang 1 ; Liu, Yanjun 1 ; Zhang, Delin 1 ; Yin, Ping 1 ; Ma, Ling 1 ; Liu, Zhu 1 ;

作者机构： 1.Huazhong Agr Univ, Natl Key Lab Crop Genet Improvement, Hubei Hongshan Lab, Wuhan, Peoples R China

2.Zhejiang Univ, Coll Life Sci, Hangzhou, Peoples R China

3.Chinese Acad Agr Sci, Agr Genom Inst Shenzhen, Shenzhen Branch, Guangdong Lab Lingnan Modern Agr,Genome Anal Lab,M, Shenzhen, Peoples R China

期刊名称：NATURE COMMUNICATIONS （ 影响因子：15.7； 五年影响因子：17.2 ）

ISSN：

年卷期： 2025 年 16 卷 1 期

页码：

收录情况： SCI

摘要： XPR1 is the sole protein known to transport inorganic phosphate (Pi) out of cells, a function conserved across species from yeast to mammals. Human XPR1 variants lead to cerebral calcium-phosphate deposition and primary familial brain calcification (PFBC), a hereditary neurodegenerative disorder. Here, we present the cryo-EM structure of human XPR1 in both its Pi-unbound and various Pi-bound states. XPR1 features 10 transmembrane alpha-helices forming an ion channel-like structure, with multiple Pi recognition sites along the channel. Pathogenic mutations in two arginine residues, which line the translocation channel, disrupt Pi transport. Molecular dynamics simulations reveal that Pi ion undergoes a stepwise transition through the sequential recognition sites during the transport process. Together with functional analyses, our results suggest that this sequential arrangement allows XPR1 to facilitate Pi ion passage via a "relay" process, and they establish a framework for the interpretation of disease-related mutations and for the development of future therapeutics.

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