ArticlePflugers Archiv : European journal of physiology2016
Human CNNM2 is not a Mg(2+) transporter per se.
Article in Pflugers Archiv : European journal of physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 41 citations in OpenAlex.
- The PACT Network: PRL, ARL, CNNM, and TRPM Proteins in Magnesium Transport and Disease.International journal of molecular sciences · 2025Review
- Prebiotics as modulators of colonic calcium and magnesium uptake.Acta physiologica (Oxford, England) · 2025Review
- Two novel variants inFrontiers in genetics · 2025Article
- Article
- NovelFrontiers in genetics · 2022Article
- CNNM proteins selectively bind to the TRPM7 channel to stimulate divalent cation entry into cells.PLoS biology · 2021Article
- Diseases caused by mutations in the NaAmerican journal of physiology. Cell physiology · 2021Review
- Article
- The Combined Influence of Magnesium and Insulin on Central Metabolic Functions and Expression of Genes Involved in Magnesium Homeostasis of Cultured Bovine Adipocytes.International journal of molecular sciences · 2021Article
- Cyclin M2 (CNNM2) knockout mice show mild hypomagnesaemia and developmental defects.Scientific reports · 2021Article
- MgNutrients · 2021Review
- Article
- General Aspects of Metal Ions as Signaling Agents in Health and Disease.Biomolecules · 2020Review
- The Role of Disturbed Mg Homeostasis in Chronic Kidney Disease Comorbidities.Frontiers in cell and developmental biology · 2020Review
- Structural Insights into the Intracellular Region of the Human Magnesium Transport Mediator CNNM4.International journal of molecular sciences · 2019Article
- Current Structural Knowledge on the CNNM Family of Magnesium Transport Mediators.International journal of molecular sciences · 2019Review
- Renal sodium and magnesium reabsorption are not coupled in a mouse model of Gordon syndrome.Physiological reports · 2018Article
- CrossTalk opposing view: CNNM proteins are not NaThe Journal of physiology · 2018Article
- Rebuttal from Francisco J. Arjona and Jeroen H. F. de Baaij.The Journal of physiology · 2018Article
- Rebuttal from Yosuke Funato, Kazuharu Furutani, Yoshihisa Kurachi and Hiroaki Miki.The Journal of physiology · 2018Article
Corrections and comments
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Authors and funding
14 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CNNM2 is associated with the regulation of serum Mg concentration, and when mutated, with severe familial hypomagnesemia. The function and cellular localization of CNNM2 and its isomorphs (Iso) remain controversial. The objective of this work was to examine the following: (1) the transcription-responsiveness of CNNM2 to Mg starvation, (2) the cellular localization of Iso1 and Iso2, (3) the ability of Iso1 and Iso2 to transport Mg(2+), and (4) the complex-forming ability and spectra of potential interactors of Iso1 and Iso2. The five main findings are as follows. (1) Mg-starvation induces CNNM2 overexpression that is markedly higher in JVM-13 cells (lymphoblasts) compared with Jurkat cells (T-lymphocytes). (2) Iso1 and Iso2 localize throughout various subcellular compartments in transgenic HEK293 cells overexpressing Iso1 or Iso2. (3) Iso1 and Iso2 do not transport Mg(2+) in an electrogenic or electroneutral mode in transgenic HEK293 cells overexpressing Iso1 or Iso2. (4) Both Iso1 and Iso2 form complexes of a higher molecular order. (5) The spectrum of potential interactors of Iso1 is ten times smaller than that of Iso2. We conclude that sensitivity of CNNM2 expression to extracellular Mg(2+) depletion depends on cell type. Iso1 and Iso2 exhibit a dispersed pattern of cellular distribution; thus, they are not exclusively integral to the cytoplasmic membrane. Iso1 and Iso2 are not Mg(2+) transporters per se. Both isomorphs form protein complexes, and divergent spectra of potential interactors of Iso1 and Iso2 indicate that each isomorph has a distinctive function. CNNM2 is therefore the first ever identified Mg(2+) homeostatic factor without being a Mg(2+) transporter per se.
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