ArticleMolecular cell2025
KIDINS220 and InsP8 safeguard the stepwise regulation of phosphate exporter XPR1.
Article in Molecular cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates.FEBS letters · 2026Review
- The PHO1 protein family in phosphate export and beyond.Plant physiology · 2026Review
- When can AlphaFold predict the oligomeric states of proteins?Protein science : a publication of the Protein Society · 2026Article
- Construction and validation of a machine learning model to predict the sarcopenic obesity population.Medicine · 2026Article
- Proteome-wide quantification of inositol pyrophosphate-protein interactions.Nature communications · 2026Article
- The SPX protein family in plants: from phosphate sensors to multifunctional signaling hubs.Stress biology · 2026Review
- Structural insights into the gating mechanism of the fission yeast phosphate exporter SpXpr1.Cell discovery · 2026Article
- Combined Targeted Drug Delivery Systems for Mineral Metabolism Disorders in Chronic Kidney Disease: A Narrative Review.International journal of nanomedicine · 2026Review
- TGFβ signaling regulates the response of the skeleton to phosphate.bioRxiv : the preprint server for biology · 2025Article
- The identification of XPR1 as a voltage- and phosphate-activated phosphate-permeable ion channel.Nature communications · 2025Article
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Authors and funding
14 authors.
Funding
Abstract
XPR1 is emerging as the only known inorganic phosphate (Pi) exporter in humans, critical for Pi homeostasis, with its activity stimulated by inositol pyrophosphate InsP8 and regulated by neuronal scaffold protein KIDINS220. Our structural studies reveal that InsP8 specifically activates XPR1 in a stepwise manner, involving profound SYG1/PHO/XPR1 (SPX) domain movements. Each XPR1 subunit functions with four gating states, in which Pi permeates a constriction site via a "knock-kiss-kick" process. By contrast, KIDINS220 delicately stabilizes XPR1 in a closed conformation through multiple mechanisms, one of which involves trapping the XPR1 α1 helix-critical for InsP8 binding-within an interaction hub. InsP8 serves as a key to release KIDINS220's restraint, reinforcing a "key-to-locks" mechanism to safeguard the stepwise activation. Additionally, our study provides direct structural insights into XPR1-associated neuronal disorders and highlights the evolutionary conservation and divergence among XPR1 orthologs, offering a comprehensive understanding of Pi homeostasis across species.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.