Structural insights into regulation of TRPM7 divalent cation uptake by the small GTPase ARL15.
| العنوان: | Structural insights into regulation of TRPM7 divalent cation uptake by the small GTPase ARL15. |
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| المؤلفون: | Mahbub L; Department of Biochemistry, McGill University, Montréal, Canada.; Centre de recherche en biologie structurale, McGill University, Montréal, Canada., Kozlov G; Department of Biochemistry, McGill University, Montréal, Canada.; Centre de recherche en biologie structurale, McGill University, Montréal, Canada., Zong P; Dept. of Cell Biology. UCONN Health Center, Farmington, Connecticut, United States., Tetteh S; Rutgers-Robert Wood Johnson Medical School, Piscataway, New Jersey, United States., Nethramangalath T; Rutgers-Robert Wood Johnson Medical School, Piscataway, New Jersey, United States., Knorn C; Department of Biochemistry, McGill University, Montréal, Canada.; Centre de recherche en biologie structurale, McGill University, Montréal, Canada., Jiang J; Department of Biochemistry, McGill University, Montréal, Canada.; Centre de recherche en biologie structurale, McGill University, Montréal, Canada., Shahsavan A; Department of Biochemistry, McGill University, Montréal, Canada.; Centre de recherche en biologie structurale, McGill University, Montréal, Canada., Lee E; Department of Biochemistry, McGill University, Montréal, Canada.; Centre de recherche en biologie structurale, McGill University, Montréal, Canada., Yue L; Dept. of Cell Biology. UCONN Health Center, Farmington, Connecticut, United States., Runnels LW; Rutgers-Robert Wood Johnson Medical School, Piscataway, New Jersey, United States., Gehring K; Department of Biochemistry, McGill University, Montréal, Canada.; Centre de recherche en biologie structurale, McGill University, Montréal, Canada. |
| المصدر: | BioRxiv : the preprint server for biology [bioRxiv] 2023 Jan 20. Date of Electronic Publication: 2023 Jan 20. |
| نوع المنشور: | Preprint |
| اللغة: | English |
| بيانات الدورية: | Country of Publication: United States NLM ID: 101680187 Publication Model: Electronic Cited Medium: Internet NLM ISO Abbreviation: bioRxiv Subsets: PubMed not MEDLINE |
| مستخلص: | Cystathionine-β-synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) are an evolutionarily conserved family of magnesium transporters. They promote efflux of Mg 2+ ions on their own or uptake of divalent cations when coupled to the transient receptor potential ion channel subfamily M member 7 (TRPM7). Recently, ADP-ribosylation factor-like GTPase 15 (ARL15) has been identified as CNNM binding partner and an inhibitor of divalent cation influx by TRPM7. Here, we characterize ARL15 as a GTP-binding protein and demonstrate that it binds the CNNM CBS-pair domain with low micromolar affinity. The crystal structure of the complex between ARL15 GTPase domain and CNNM2 CBS-pair domain reveals the molecular determinants of the interaction and allowed the identification of mutations in ARL15 and CNNM2 mutations that abrogate binding. Loss of CNNM binding prevented ARL15 suppression of TRPM7 channel activity in support of previous reports that the proteins function as a ternary complex. Binding experiments with phosphatase of regenerating liver 2 (PRL2 or PTP4A2) revealed that ARL15 and PRLs compete for binding CNNM, suggesting antagonistic regulation of divalent cation transport by the two proteins. |
| التعليقات: | Update in: Elife. 2023 Jul 14;12:. (PMID: 37449820) |
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| معلومات مُعتمدة: | R01 HL147350 United States HL NHLBI NIH HHS |
| تواريخ الأحداث: | Date Created: 20230130 Latest Revision: 20230717 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC9882303 |
| DOI: | 10.1101/2023.01.19.524765 |
| PMID: | 36711628 |
| قاعدة البيانات: | MEDLINE |
| DOI: | 10.1101/2023.01.19.524765 |
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