Structural and functional comparison of magnesium transporters throughout evolution
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...
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| Veröffentlicht in: | Cellular and molecular life sciences : CMLS 2022-08, Vol.79 (8), p.418-418, Article 418 |
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| description | 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. |
| doi_str_mv | 10.1007/s00018-022-04442-8 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9276622</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2688282422</sourcerecordid><originalsourceid>FETCH-LOGICAL-c500t-edee3dd2582915c78fce42dd7949d7bbafce020299ed359200c9b21835855a3c3</originalsourceid><addsrcrecordid>eNp9kUtr3DAUhUVoyKv9A10ZuunG6dW1ZUubQglpUghkkQSyExpJnnGwpYkeA_33VeKhoV1kde9F3zkcdAj5TOGcAvTfIgBQXgNiDW3bYs0PyAltEWoBPf2w3zuOj8fkNManQjOO3RE5bhingjXshNzdpZB1ykFNlXKmGrLTafSunNrPWxXG6F3lh2pWa2fjmOcqBeXi1odkQ6zSJvi83vicKrvzU37RfiSHg5qi_bSfZ-Th5-X9xXV9c3v16-LHTa0ZQKqtsbYxBksmQZnu-aBti8b0ohWmX61UuQEBhbCmYQIBtFgh5SU8Y6rRzRn5vvhu82q2RltXok1yG8ZZhd_Sq1H---LGjVz7nRTYdx1iMfi6Nwj-OduY5DxGbadJOetzlNhxzjrOoC_ol__QJ59D-aaFQo7tqyEulA4-xmCHv2EoyJfO5NKZLJ3J184kL6JmEcUCu7UNb9bvqP4AdX2a4w</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2688282422</pqid></control><display><type>article</type><title>Structural and functional comparison of magnesium transporters throughout evolution</title><source>SpringerNature Journals</source><source>PubMed Central</source><creator>Franken, G. A. C. ; Huynen, M. A. ; Martínez-Cruz, L. A. ; Bindels, R. J. M. ; de Baaij, J. H. F.</creator><creatorcontrib>Franken, G. A. C. ; Huynen, M. A. ; Martínez-Cruz, L. A. ; Bindels, R. J. M. ; de Baaij, J. H. F.</creatorcontrib><description>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.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-022-04442-8</identifier><identifier>PMID: 35819535</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Cell Biology ; Channels ; DNA biosynthesis ; Efflux ; Eukaryotes ; Evolution ; Homeostasis ; Intracellular ; Kinases ; Life Sciences ; Magnesium ; Prokaryotes ; Protein biosynthesis ; Protein structure ; Protein synthesis ; Proteins ; Quaternary structure ; Review ; Selectivity ; Structure-function relationships ; Transient receptor potential proteins ; Vertebrates</subject><ispartof>Cellular and molecular life sciences : CMLS, 2022-08, Vol.79 (8), p.418-418, Article 418</ispartof><rights>The Author(s) 2022</rights><rights>The Author(s) 2022. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c500t-edee3dd2582915c78fce42dd7949d7bbafce020299ed359200c9b21835855a3c3</citedby><cites>FETCH-LOGICAL-c500t-edee3dd2582915c78fce42dd7949d7bbafce020299ed359200c9b21835855a3c3</cites><orcidid>0000-0003-2372-8486</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9276622/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9276622/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,729,782,786,887,27931,27932,41495,42564,51326,53798,53800</link.rule.ids></links><search><creatorcontrib>Franken, G. A. C.</creatorcontrib><creatorcontrib>Huynen, M. A.</creatorcontrib><creatorcontrib>Martínez-Cruz, L. A.</creatorcontrib><creatorcontrib>Bindels, R. J. M.</creatorcontrib><creatorcontrib>de Baaij, J. H. F.</creatorcontrib><title>Structural and functional comparison of magnesium transporters throughout evolution</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell. Mol. Life Sci</addtitle><description>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.</description><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cell Biology</subject><subject>Channels</subject><subject>DNA biosynthesis</subject><subject>Efflux</subject><subject>Eukaryotes</subject><subject>Evolution</subject><subject>Homeostasis</subject><subject>Intracellular</subject><subject>Kinases</subject><subject>Life Sciences</subject><subject>Magnesium</subject><subject>Prokaryotes</subject><subject>Protein biosynthesis</subject><subject>Protein structure</subject><subject>Protein synthesis</subject><subject>Proteins</subject><subject>Quaternary structure</subject><subject>Review</subject><subject>Selectivity</subject><subject>Structure-function relationships</subject><subject>Transient receptor potential proteins</subject><subject>Vertebrates</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kUtr3DAUhUVoyKv9A10ZuunG6dW1ZUubQglpUghkkQSyExpJnnGwpYkeA_33VeKhoV1kde9F3zkcdAj5TOGcAvTfIgBQXgNiDW3bYs0PyAltEWoBPf2w3zuOj8fkNManQjOO3RE5bhingjXshNzdpZB1ykFNlXKmGrLTafSunNrPWxXG6F3lh2pWa2fjmOcqBeXi1odkQ6zSJvi83vicKrvzU37RfiSHg5qi_bSfZ-Th5-X9xXV9c3v16-LHTa0ZQKqtsbYxBksmQZnu-aBti8b0ohWmX61UuQEBhbCmYQIBtFgh5SU8Y6rRzRn5vvhu82q2RltXok1yG8ZZhd_Sq1H---LGjVz7nRTYdx1iMfi6Nwj-OduY5DxGbadJOetzlNhxzjrOoC_ol__QJ59D-aaFQo7tqyEulA4-xmCHv2EoyJfO5NKZLJ3J184kL6JmEcUCu7UNb9bvqP4AdX2a4w</recordid><startdate>20220801</startdate><enddate>20220801</enddate><creator>Franken, G. A. C.</creator><creator>Huynen, M. A.</creator><creator>Martínez-Cruz, L. A.</creator><creator>Bindels, R. J. M.</creator><creator>de Baaij, J. H. 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A. C. ; Huynen, M. A. ; Martínez-Cruz, L. A. ; Bindels, R. J. M. ; de Baaij, J. H. 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A. C.</au><au>Huynen, M. A.</au><au>Martínez-Cruz, L. A.</au><au>Bindels, R. J. M.</au><au>de Baaij, J. H. F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural and functional comparison of magnesium transporters throughout evolution</atitle><jtitle>Cellular and molecular life sciences : CMLS</jtitle><stitle>Cell. Mol. Life Sci</stitle><date>2022-08-01</date><risdate>2022</risdate><volume>79</volume><issue>8</issue><spage>418</spage><epage>418</epage><pages>418-418</pages><artnum>418</artnum><issn>1420-682X</issn><eissn>1420-9071</eissn><abstract>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.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>35819535</pmid><doi>10.1007/s00018-022-04442-8</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0003-2372-8486</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Cellular and molecular life sciences : CMLS, 2022-08, Vol.79 (8), p.418-418, Article 418 |
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| language | eng |
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| source | SpringerNature Journals; PubMed Central |
| subjects | Biochemistry Biomedical and Life Sciences Biomedicine Cell Biology Channels DNA biosynthesis Efflux Eukaryotes Evolution Homeostasis Intracellular Kinases Life Sciences Magnesium Prokaryotes Protein biosynthesis Protein structure Protein synthesis Proteins Quaternary structure Review Selectivity Structure-function relationships Transient receptor potential proteins Vertebrates |
| title | Structural and functional comparison of magnesium transporters throughout evolution |
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