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Article ; Online: Impact of Zinc Transport Mechanisms on Embryonic and Brain Development.

Willekens, Jeremy / Runnels, Loren W

2022 Volume 14, Issue 12

Abstract: The trace element zinc (Zn) binds to over ten percent of proteins in eukaryotic cells. Zn flexible chemistry allows it to regulate the activity of hundreds of enzymes and influence scores of metabolic processes in cells throughout the body. Deficiency of ...

Abstract	The trace element zinc (Zn) binds to over ten percent of proteins in eukaryotic cells. Zn flexible chemistry allows it to regulate the activity of hundreds of enzymes and influence scores of metabolic processes in cells throughout the body. Deficiency of Zn in humans has a profound effect on development and in adults later in life, particularly in the brain, where Zn deficiency is linked to several neurological disorders. In this review, we will summarize the importance of Zn during development through a description of the outcomes of both genetic and early dietary Zn deficiency, focusing on the pathological consequences on the whole body and brain. The epidemiology and the symptomology of Zn deficiency in humans will be described, including the most studied inherited Zn deficiency disease,
MeSH term(s)	Acrodermatitis/metabolism ; Animals ; Brain/metabolism ; Cation Transport Proteins/genetics ; Cation Transport Proteins/metabolism ; Female ; Pregnancy ; Zinc/deficiency
Chemical Substances	Cation Transport Proteins ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2022-06-17
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2518386-2
ISSN	2072-6643 ; 2072-6643
ISSN (online)	2072-6643
ISSN	2072-6643
DOI	10.3390/nu14122526
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Article: Impact of Zinc Transport Mechanisms on Embryonic and Brain Development

Willekens, Jeremy / Runnels, Loren W.

Nutrients. 2022 June 17, v. 14, no. 12

2022

Abstract	The trace element zinc (Zn) binds to over ten percent of proteins in eukaryotic cells. Zn flexible chemistry allows it to regulate the activity of hundreds of enzymes and influence scores of metabolic processes in cells throughout the body. Deficiency of Zn in humans has a profound effect on development and in adults later in life, particularly in the brain, where Zn deficiency is linked to several neurological disorders. In this review, we will summarize the importance of Zn during development through a description of the outcomes of both genetic and early dietary Zn deficiency, focusing on the pathological consequences on the whole body and brain. The epidemiology and the symptomology of Zn deficiency in humans will be described, including the most studied inherited Zn deficiency disease, Acrodermatitis enteropathica. In addition, we will give an overview of the different forms and animal models of Zn deficiency, as well as the 24 Zn transporters, distributed into two families: the ZIPs and the ZnTs, which control the balance of Zn throughout the body. Lastly, we will describe the TRPM7 ion channel, which was recently shown to contribute to intestinal Zn absorption and has its own significant impact on early embryonic development.
Keywords	absorption ; acrodermatitis ; brain ; embryogenesis ; epidemiology ; intestines ; ion channels ; zinc
Language	English
Dates of publication	2022-0617
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2518386-2
ISSN	2072-6643
ISSN	2072-6643
DOI	10.3390/nu14122526
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Article ; Online: TRPM6 and TRPM7: Novel players in cell intercalation during vertebrate embryonic development.

Runnels, Loren W / Komiya, Yuko

Developmental dynamics : an official publication of the American Association of Anatomists

2020 Volume 249, Issue 8, Page(s) 912–923

Abstract: A common theme in organogenesis is how the final structure of organs emerge from epithelial tube structures, with the formation of the neural tube being one of the best examples. Two types of cell movements co-occur during neural tube closure involving ... ...

Abstract	A common theme in organogenesis is how the final structure of organs emerge from epithelial tube structures, with the formation of the neural tube being one of the best examples. Two types of cell movements co-occur during neural tube closure involving the migration of cells toward the midline of the embryo (mediolateral intercalation or convergent extension) as well as the deep movement of cells from inside the embryo to the outside of the lateral side of the neural plate (radial intercalation). Failure of either type of cell movement will prevent neural tube closure, which can produce a range of neural tube defects (NTDs), a common congenital disease in humans. Numerous studies have identified signaling pathways that regulate mediolateral intercalation during neural tube closure. Less understood are the pathways that govern radial intercalation. Using the Xenopus laevis system, our group reported the identification of transient receptor potential (TRP) channels, TRPM6 and TRPM7, and the Mg
MeSH term(s)	3T3 Cells ; Animals ; Cell Movement ; Embryonic Development ; Gene Expression Regulation, Developmental ; Humans ; Ions ; Magnesium/chemistry ; Magnesium/metabolism ; Mice ; Neural Plate/metabolism ; Neural Tube/metabolism ; Neural Tube Defects/genetics ; Neural Tube Defects/metabolism ; Neurulation ; Protein Domains ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/physiology ; Signal Transduction ; TRPM Cation Channels/genetics ; TRPM Cation Channels/metabolism ; TRPM Cation Channels/physiology ; Xenopus Proteins/genetics ; Xenopus Proteins/physiology ; Xenopus laevis/metabolism ; Zebrafish
Chemical Substances	Ions ; TRPM Cation Channels ; TRPM6 protein, human ; TRPM7 protein, Xenopus ; Trpm6 protein, mouse ; Xenopus Proteins ; Trpm7 protein, mouse (EC 2.7.1.-) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; TRPM7 protein, human (EC 2.7.11.1) ; Magnesium (I38ZP9992A)
Language	English
Publishing date	2020-05-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1102541-4
ISSN	1097-0177 ; 1058-8388
ISSN (online)	1097-0177
ISSN	1058-8388
DOI	10.1002/dvdy.182
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Article: Structural insights into regulation of TRPM7 divalent cation uptake by the small GTPase ARL15.

Mahbub, Luba / Kozlov, Guennadi / Zong, Pengyu / Tetteh, Sandra / Nethramangalath, Thushara / Knorn, Caroline / Jiang, Jianning / Shahsavan, Ashkan / Lee, Emma / Yue, Lixia / Runnels, Loren W / Gehring, Kalle

bioRxiv : the preprint server for biology

2023

Abstract: Cystathionine-β-synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) are an evolutionarily conserved family of magnesium transporters. They promote efflux of ... ...

Abstract	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
Language	English
Publishing date	2023-01-20
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.01.19.524765
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Article ; Online: TRPM6 and TRPM7: A Mul-TRP-PLIK-cation of channel functions.

Runnels, Loren W

Current pharmaceutical biotechnology

2010 Volume 12, Issue 1, Page(s) 42–53

Abstract: Unique among ion channels, TRPM6 and TRPM7 garnered much interest upon their discovery as the first ion channels to possess their own kinase domain. Soon after their identification, the two proteins were quickly linked to the regulation of magnesium ... ...

Abstract	Unique among ion channels, TRPM6 and TRPM7 garnered much interest upon their discovery as the first ion channels to possess their own kinase domain. Soon after their identification, the two proteins were quickly linked to the regulation of magnesium homeostasis. However, study of their physiological functions in mouse and zebrafish have revealed expanding roles for these channel-kinases that include skeletogenesis and melanopore formation, thymopoiesis, cell adhesion, and neural fold closure during early development. In addition, mutations in the TRPM6 gene constitute the underlying genetic defect in hypomagnesemia with secondary hypocalcemia, a rare autosomal-recessive disease characterized by low serum magnesium accompanied by hypocalcemia. Depletion of TRPM7 expression in brain, on the other hand, proved successful in mitigating much of the cellular devastation that accompanies oxygen-glucose deprivation during ischemia. The aim of this review is to summarize the data emerging from molecular genetic, biochemical, electrophysiological, and pharmacological studies of these unique channel-kinases.
MeSH term(s)	Animals ; Cations/metabolism ; Cell Growth Processes ; Disease Models, Animal ; HEK293 Cells ; Homeostasis ; Humans ; Ion Channels/metabolism ; Magnesium/blood ; Magnesium/metabolism ; Mice ; Nuclear Proteins/agonists ; Nuclear Proteins/antagonists & inhibitors ; Nuclear Proteins/metabolism ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases ; TRPM Cation Channels/agonists ; TRPM Cation Channels/antagonists & inhibitors ; TRPM Cation Channels/genetics ; TRPM Cation Channels/metabolism ; Tripartite Motif Proteins ; Ubiquitin-Protein Ligases
Chemical Substances	Cations ; Ion Channels ; Nuclear Proteins ; TRPM Cation Channels ; TRPM6 protein, human ; Tripartite Motif Proteins ; TRIM37 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Protein Kinases (EC 2.7.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; TRPM7 protein, human (EC 2.7.11.1) ; Magnesium (I38ZP9992A)
Language	English
Publishing date	2010-10-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2132197-8
ISSN	1873-4316 ; 1389-2010
ISSN (online)	1873-4316
ISSN	1389-2010
DOI	10.2174/138920111793937880
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Article ; Online: TRPM channels and magnesium in early embryonic development.

Komiya, Yuko / Runnels, Loren W

The International journal of developmental biology

2015 Volume 59, Issue 7-9, Page(s) 281–288

Abstract: Magnesium (Mg(2+)) is the second most abundant cellular cation and is essential for all stages of life, from the early embryo to adult. Mg(2+) deficiency causes or contributes to many human diseases, including migraine headaches, Parkinson's disease, ... ...

Abstract	Magnesium (Mg(2+)) is the second most abundant cellular cation and is essential for all stages of life, from the early embryo to adult. Mg(2+) deficiency causes or contributes to many human diseases, including migraine headaches, Parkinson's disease, Alzheimer's disease, hypotension, type 2 diabetes mellitus and cardiac arrhythmias. Although the concentration of Mg(2+) in the extracellular environment can vary significantly, the total intracellular Mg(2+) concentration is actively maintained within a relatively narrow range (14 - 20 mM) via tight, yet poorly understood, regulation of intracellular Mg(2+)by Mg(2+) transporters and Mg(2+)-permeant ion channels. Recent studies have continued to add to the growing number of Mg(2+) transporters and ion channels involved in Mg(2+) homeostasis, including TRPM6 and TRPM7, members of the transient receptor potential (TRP) ion channel family. Mutations in TRPM6, including amino acid substitutions that prevent its heterooligomerization with TRPM7, occur in the rare autosomal-recessive disease hypomagnesemia with secondary hypocalcemia (HSH). Genetic ablation of either gene in mice results in early embryonic lethality, raising the question of whether these channels' capacity to mediate Mg(2+) influx plays an important role in embryonic development. Here we review what is known of the function of Mg(2+) in early development and summarize recent findings regarding the function of the TRPM6 and TRPM7 ion channels during embryogenesis.
MeSH term(s)	Animals ; Embryonic Development/physiology ; Magnesium/metabolism ; Mice ; Mice, Knockout ; TRPM Cation Channels/metabolism
Chemical Substances	TRPM Cation Channels ; Magnesium (I38ZP9992A)
Language	English
Publishing date	2015
Publishing country	Spain
Document type	Journal Article ; Review
ZDB-ID	1036070-0
ISSN	1696-3547 ; 0214-6282
ISSN (online)	1696-3547
ISSN	0214-6282
DOI	10.1387/ijdb.150196lr
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Article ; Online: Ca

Feng, Jianlin / Armillei, Maria K / Yu, Albert S / Liang, Bruce T / Runnels, Loren W / Yue, Lixia

Journal of cardiovascular development and disease

2019 Volume 6, Issue 4

Abstract: Cardiac fibrosis is the excessive deposition of extracellular matrix proteins by cardiac fibroblasts and myofibroblasts, and is a hallmark feature of most heart diseases, including arrhythmia, hypertrophy, and heart failure. This maladaptive process ... ...

Abstract	Cardiac fibrosis is the excessive deposition of extracellular matrix proteins by cardiac fibroblasts and myofibroblasts, and is a hallmark feature of most heart diseases, including arrhythmia, hypertrophy, and heart failure. This maladaptive process occurs in response to a variety of stimuli, including myocardial injury, inflammation, and mechanical overload. There are multiple signaling pathways and various cell types that influence the fibrogenesis cascade. Fibroblasts and myofibroblasts are central effectors. Although it is clear that Ca
Language	English
Publishing date	2019-09-23
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2777082-5
ISSN	2308-3425 ; 2308-3425
ISSN (online)	2308-3425
ISSN	2308-3425
DOI	10.3390/jcdd6040034
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Article ; Online: Mass Spectrometric Analysis of TRPM6 and TRPM7 Phosphorylation Reveals Regulatory Mechanisms of the Channel-Kinases.

Cai, Na / Bai, Zhiyong / Nanda, Vikas / Runnels, Loren W

Scientific reports

2017 Volume 7, Page(s) 42739

Abstract: TRPM7 and TRPM6 were the first identified bifunctional channels to contain their own kinase domains, but how these channel-kinases are regulated is poorly understood. Previous studies identified numerous phosphorylation sites on TRPM7, but very little is ...

Abstract	TRPM7 and TRPM6 were the first identified bifunctional channels to contain their own kinase domains, but how these channel-kinases are regulated is poorly understood. Previous studies identified numerous phosphorylation sites on TRPM7, but very little is known about TRPM6 phosphorylation or sites on TRPM7 transphosphorylated by TRPM6. Our mass spectrometric analysis of homomeric and heteromeric TRPM7 and TRPM6 channels identified phosphorylation sites on both proteins, as well as several prominent sites on TRPM7 that are commonly modified through autophosphorylation and transphosphorylation by TRPM6. We conducted a series of amino acid substitution analyses and identified S1777, in TRPM7's catalytic domain, and S1565, in TRPM7's exchange domain that mediates kinase dimerization, as potential regulatory sites. The phosphomimetic S1777D substitution disrupted catalytic activity, most likely by causing an electrostatic perturbation at the active site. The S1565D phosphomimetic substitution also inactivated the kinase but did so without interfering with kinase dimerization. Molecular modeling indicates that phosphorylation of S1565 is predicted to structurally affect TRPM7's functionally conserved N/D loop, which is thought to influence the access of substrate to the active site pocket. We propose that phosphorylation of S1565 within the exchange domain functions as a regulatory switch to control TRPM7 catalytic activity.
MeSH term(s)	Amino Acid Substitution ; Catalytic Domain ; HEK293 Cells ; Humans ; Phosphorylation ; Protein Multimerization ; Protein Processing, Post-Translational ; Protein-Serine-Threonine Kinases/chemistry ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; TRPM Cation Channels/chemistry ; TRPM Cation Channels/genetics ; TRPM Cation Channels/metabolism
Chemical Substances	TRPM Cation Channels ; TRPM6 protein, human ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; TRPM7 protein, human (EC 2.7.11.1)
Language	English
Publishing date	2017-02-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/srep42739
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Article ; Online: The kinase activity of the channel-kinase protein TRPM7 regulates stability and localization of the TRPM7 channel in polarized epithelial cells.

Cai, Na / Lou, Liping / Al-Saadi, Namariq / Tetteh, Sandra / Runnels, Loren W

The Journal of biological chemistry

2018 Volume 293, Issue 29, Page(s) 11491–11504

Abstract: The channel-kinase transient receptor potential melastatin 7 (TRPM7) is a bifunctional protein with ion channel and kinase domains. The kinase activity of TRPM7 has been linked to the regulation of a broad range of cellular activities, but little is ... ...

Abstract	The channel-kinase transient receptor potential melastatin 7 (TRPM7) is a bifunctional protein with ion channel and kinase domains. The kinase activity of TRPM7 has been linked to the regulation of a broad range of cellular activities, but little is understood as to how the channel itself is regulated by its own kinase activity. Here, using several mammalian cell lines expressing WT TRPM7 or kinase-inactive variants, we discovered that compared with the cells expressing WT TRPM7, cells in which TRPM7's kinase activity was inactivated had faster degradation, elevated ubiquitination, and increased intracellular retention of the channel. Mutational analysis of TRPM7 autophosphorylation sites further revealed a role for Ser-1360 of TRPM7 as a key residue mediating both TRPM7 stability and intracellular trafficking. Additional trafficking roles were uncovered for Ser-1403 and Ser-1567, whose phosphorylation by TRPM7's kinase activity mediated the interaction of the channel with the signaling protein 14-3-3θ. In summary, our results point to a critical role for TRPM7's kinase activity in regulating proteasome-mediated turnover of the TRPM7 channel and controlling its cellular localization in polarized epithelial cells. Overall, these findings improve our understanding of the significance of TRPM7's kinase activity for functional regulation of its channel activity.
MeSH term(s)	14-3-3 Proteins/metabolism ; Animals ; Cell Polarity ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; HEK293 Cells ; Humans ; Mice ; Phosphorylation ; Protein Binding ; Protein Kinases/analysis ; Protein Kinases/metabolism ; Protein Stability ; Protein Transport ; TRPM Cation Channels/analysis ; TRPM Cation Channels/metabolism
Chemical Substances	14-3-3 Proteins ; TRPM Cation Channels ; Protein Kinases (EC 2.7.-) ; Trpm7 protein, mouse (EC 2.7.1.-)
Language	English
Publishing date	2018-06-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA118.001925
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Article ; Online: CNNM proteins selectively bind to the TRPM7 channel to stimulate divalent cation entry into cells.

Bai, Zhiyong / Feng, Jianlin / Franken, Gijs A C / Al'Saadi, Namariq / Cai, Na / Yu, Albert S / Lou, Liping / Komiya, Yuko / Hoenderop, Joost G J / de Baaij, Jeroen H F / Yue, Lixia / Runnels, Loren W

PLoS biology

2021 Volume 19, Issue 12, Page(s) e3001496

Abstract: Magnesium is essential for cellular life, but how it is homeostatically controlled still remains poorly understood. Here, we report that members of CNNM family, which have been controversially implicated in both cellular Mg2+ influx and efflux, ... ...

Abstract	Magnesium is essential for cellular life, but how it is homeostatically controlled still remains poorly understood. Here, we report that members of CNNM family, which have been controversially implicated in both cellular Mg2+ influx and efflux, selectively bind to the TRPM7 channel to stimulate divalent cation entry into cells. Coexpression of CNNMs with the channel markedly increased uptake of divalent cations, which is prevented by an inactivating mutation to the channel's pore. Knockout (KO) of TRPM7 in cells or application of the TRPM7 channel inhibitor NS8593 also interfered with CNNM-stimulated divalent cation uptake. Conversely, KO of CNNM3 and CNNM4 in HEK-293 cells significantly reduced TRPM7-mediated divalent cation entry, without affecting TRPM7 protein expression or its cell surface levels. Furthermore, we found that cellular overexpression of phosphatases of regenerating liver (PRLs), known CNNMs binding partners, stimulated TRPM7-dependent divalent cation entry and that CNNMs were required for this activity. Whole-cell electrophysiological recordings demonstrated that deletion of CNNM3 and CNNM4 from HEK-293 cells interfered with heterologously expressed and native TRPM7 channel function. We conclude that CNNMs employ the TRPM7 channel to mediate divalent cation influx and that CNNMs also possess separate TRPM7-independent Mg2+ efflux activities that contribute to CNNMs' control of cellular Mg2+ homeostasis.
MeSH term(s)	Cation Transport Proteins/metabolism ; Cation Transport Proteins/physiology ; Cations, Divalent/metabolism ; Cell Line, Tumor ; Cyclins/metabolism ; Cyclins/physiology ; HEK293 Cells ; Humans ; Magnesium/metabolism ; Patch-Clamp Techniques ; Protein Serine-Threonine Kinases/metabolism ; Protein Serine-Threonine Kinases/physiology ; TRPM Cation Channels/genetics ; TRPM Cation Channels/metabolism ; TRPM Cation Channels/physiology
Chemical Substances	CNNM3 protein, human ; CNNM4 protein, human ; Cation Transport Proteins ; Cations, Divalent ; Cyclins ; TRPM Cation Channels ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; TRPM7 protein, human (EC 2.7.11.1) ; Magnesium (I38ZP9992A)
Language	English
Publishing date	2021-12-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.3001496
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