دورية أكاديمية
Structural and functional comparison of magnesium transporters throughout evolution.
| العنوان: | Structural and functional comparison of magnesium transporters throughout evolution. |
|---|---|
| المؤلفون: | Franken GAC; Department of Physiology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, P.O. Box 9101, 6500 HB, Nijmegen, The Netherlands., Huynen MA; Center for Molecular and Biomolecular Informatics, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, Nijmegen, The Netherlands., Martínez-Cruz LA; Center for Cooperative Research in Biosciences (CIC bioGUNE), Bizkaia Science and Technology Park, Derio, 48160, Bizkaia, Spain., Bindels RJM; Department of Physiology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, P.O. Box 9101, 6500 HB, Nijmegen, The Netherlands., de Baaij JHF; Department of Physiology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, P.O. Box 9101, 6500 HB, Nijmegen, The Netherlands. jeroen.debaaij@radboudumc.nl. |
| المصدر: | Cellular and molecular life sciences : CMLS [Cell Mol Life Sci] 2022 Jul 12; Vol. 79 (8), pp. 418. Date of Electronic Publication: 2022 Jul 12. |
| نوع المنشور: | Journal Article; Review |
| اللغة: | English |
| بيانات الدورية: | Publisher: Springer Country of Publication: Switzerland NLM ID: 9705402 Publication Model: Electronic Cited Medium: Internet ISSN: 1420-9071 (Electronic) Linking ISSN: 1420682X NLM ISO Abbreviation: Cell Mol Life Sci Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Basel : Springer Original Publication: Basel ; Boston : Birkhauser, c1997- |
| مواضيع طبية MeSH: | Magnesium*/metabolism , Membrane Transport Proteins*/metabolism, Biological Transport ; Cations, Divalent/metabolism ; Phosphotransferases/metabolism |
| مستخلص: | Magnesium (Mg 2+ ) is the most prevalent divalent intracellular cation. As co-factor in many enzymatic reactions, Mg 2+ is essential for protein synthesis, energy production, and DNA stability. Disturbances in intracellular Mg 2+ concentrations, therefore, unequivocally result in delayed cell growth and metabolic defects. To maintain physiological Mg 2+ levels, all organisms rely on balanced Mg 2+ influx and efflux via Mg 2+ channels and transporters. This review compares the structure and the function of prokaryotic Mg 2+ transporters and their eukaryotic counterparts. In prokaryotes, cellular Mg 2+ homeostasis is orchestrated via the CorA, MgtA/B, MgtE, and CorB/C Mg 2+ transporters. For CorA, MgtE, and CorB/C, the motifs that form the selectivity pore are conserved during evolution. These findings suggest that CNNM proteins, the vertebrate orthologues of CorB/C, also have Mg 2+ transport capacity. Whereas CorA and CorB/C proteins share the gross quaternary structure and functional properties with their respective orthologues, the MgtE channel only shares the selectivity pore with SLC41 Na + /Mg 2+ transporters. In eukaryotes, TRPM6 and TRPM7 Mg 2+ channels provide an additional Mg 2+ transport mechanism, consisting of a fusion of channel with a kinase. The unique features these TRP channels allow the integration of hormonal, cellular, and transcriptional regulatory pathways that determine their Mg 2+ transport capacity. Our review demonstrates that understanding the structure and function of prokaryotic magnesiotropic proteins aids in our basic understanding of Mg 2+ transport. (© 2022. The Author(s).) |
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| معلومات مُعتمدة: | NWO Veni 016.186.012 Nederlandse Organisatie voor Wetenschappelijk Onderzoek; EJPRD2019-40 European Joint Programme on Rare Diseases |
| فهرسة مساهمة: | Keywords: CNNM; Channel; Magnesium; SLC41; TRPM; Transporter |
| المشرفين على المادة: | 0 (Cations, Divalent) 0 (Membrane Transport Proteins) EC 2.7.- (Phosphotransferases) I38ZP9992A (Magnesium) |
| تواريخ الأحداث: | Date Created: 20220712 Date Completed: 20220714 Latest Revision: 20220822 |
| رمز التحديث: | 20221213 |
| مُعرف محوري في PubMed: | PMC9276622 |
| DOI: | 10.1007/s00018-022-04442-8 |
| PMID: | 35819535 |
| قاعدة البيانات: | MEDLINE |
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Full Text Finder | تدمد: | 1420-9071 |
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| DOI: | 10.1007/s00018-022-04442-8 |