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  1. Article: Epithelial magnesium transport by TRPM6 is essential for prenatal development and adult survival

    Chubanov, Vladimir / Zierler, Susanna

    eLife, 2016(5): e20914

    2016  

    Abstract: Mg2+ regulates many physiological processes and signalling pathways. However, little is known about the mechanisms underlying the organismal balance of Mg2+. Capitalizing on a set of newly generated mouse models, we provide an integrated mechanistic ... ...

    Institution Deutsches Institut für Ernährungsforschung Potsdam-Rehbrücke
    Abstract Mg2+ regulates many physiological processes and signalling pathways. However, little is known about the mechanisms underlying the organismal balance of Mg2+. Capitalizing on a set of newly generated mouse models, we provide an integrated mechanistic model of the regulation of organismal Mg2+ balance during prenatal development and in adult mice by the ion channel TRPM6. We show that TRPM6 activity in the placenta and yolk sac is essential for embryonic development. In adult mice, TRPM6 is required in the intestine to maintain organismal Mg2+ balance, but is dispensable in the kidney. Trpm6 inactivation in adult mice leads to a shortened lifespan, growth deficit and metabolic alterations indicative of impaired energy balance. Dietary Mg2+ supplementation not only rescues all phenotypes displayed by Trpm6-deficient adult mice, but also may extend the lifespan of wildtype mice. Hence, maintenance of organismal Mg2+ balance by TRPM6 is crucial for prenatal development and survival to adulthood.
    Language English
    Document type Article
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  2. Article ; Online: TRPM channels in health and disease.

    Chubanov, Vladimir / Köttgen, Michael / Touyz, Rhian M / Gudermann, Thomas

    Nature reviews. Nephrology

    2023  Volume 20, Issue 3, Page(s) 175–187

    Abstract: Different cell channels and transporters tightly regulate cytoplasmic levels and the intraorganelle distribution of cations. Perturbations in these processes lead to human diseases that are frequently associated with kidney impairment. The family of ... ...

    Abstract Different cell channels and transporters tightly regulate cytoplasmic levels and the intraorganelle distribution of cations. Perturbations in these processes lead to human diseases that are frequently associated with kidney impairment. The family of melastatin-related transient receptor potential (TRPM) channels, which has eight members in mammals (TRPM1-TRPM8), includes ion channels that are highly permeable to divalent cations, such as Ca
    MeSH term(s) Animals ; Humans ; TRPM Cation Channels/genetics ; TRPM Cation Channels/metabolism ; Transient Receptor Potential Channels ; Mammals/metabolism ; Protein Serine-Threonine Kinases
    Chemical Substances TRPM Cation Channels ; Transient Receptor Potential Channels ; TRPM7 protein, human (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; TRPM1 protein, human
    Language English
    Publishing date 2023-10-18
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2490366-8
    ISSN 1759-507X ; 1759-5061
    ISSN (online) 1759-507X
    ISSN 1759-5061
    DOI 10.1038/s41581-023-00777-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Lactate as a new second messenger shaping intracellular Mg

    Chubanov, Vladimir / Gudermann, Thomas

    Cell calcium

    2020  Volume 93, Page(s) 102329

    Abstract: ... ...

    Abstract Mg
    MeSH term(s) Energy Metabolism ; Lactic Acid ; Magnesium ; Mitochondrial Dynamics ; Second Messenger Systems
    Chemical Substances Lactic Acid (33X04XA5AT) ; Magnesium (I38ZP9992A)
    Language English
    Publishing date 2020-12-08
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 757687-0
    ISSN 1532-1991 ; 0143-4160
    ISSN (online) 1532-1991
    ISSN 0143-4160
    DOI 10.1016/j.ceca.2020.102329
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  4. Article ; Online: Mapping TRPM7 Function by NS8593.

    Chubanov, Vladimir / Gudermann, Thomas

    International journal of molecular sciences

    2020  Volume 21, Issue 19

    Abstract: The transient receptor potential cation channel, subfamily M, member 7 (TRPM7) is a ubiquitously expressed membrane protein, which forms a channel linked to a cytosolic protein kinase. Genetic inactivation of TRPM7 in animal models uncovered the critical ...

    Abstract The transient receptor potential cation channel, subfamily M, member 7 (TRPM7) is a ubiquitously expressed membrane protein, which forms a channel linked to a cytosolic protein kinase. Genetic inactivation of TRPM7 in animal models uncovered the critical role of TRPM7 in early embryonic development, immune responses, and the organismal balance of Zn
    MeSH term(s) 1-Naphthylamine/analogs & derivatives ; 1-Naphthylamine/chemistry ; 1-Naphthylamine/therapeutic use ; Animals ; Disease Models, Animal ; Humans ; Ion Channel Gating/drug effects ; Ion Channel Gating/genetics ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; TRPM Cation Channels/genetics ; TRPM Cation Channels/metabolism
    Chemical Substances (R)-N-(benzimidazol-2-yl)-1,2,3,4-tetrahydro-1-naphthylamine ; TRPM Cation Channels ; 1-Naphthylamine (9753I242R5) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; TRPM7 protein, human (EC 2.7.11.1)
    Language English
    Publishing date 2020-09-23
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms21197017
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Structural basis of selective TRPM7 inhibition by the anticancer agent CCT128930.

    Nadezhdin, Kirill D / Correia, Leonor / Shalygin, Alexey / Aktolun, Muhammed / Neuberger, Arthur / Gudermann, Thomas / Kurnikova, Maria G / Chubanov, Vladimir / Sobolevsky, Alexander I

    Cell reports

    2024  Volume 43, Issue 4, Page(s) 114108

    Abstract: TRP channels are implicated in various diseases, but high structural similarity between them makes selective pharmacological modulation challenging. Here, we study the molecular mechanism underlying specific inhibition of the TRPM7 channel, which is ... ...

    Abstract TRP channels are implicated in various diseases, but high structural similarity between them makes selective pharmacological modulation challenging. Here, we study the molecular mechanism underlying specific inhibition of the TRPM7 channel, which is essential for cancer cell proliferation, by the anticancer agent CCT128930 (CCT). Using cryo-EM, functional analysis, and MD simulations, we show that CCT binds to a vanilloid-like (VL) site, stabilizing TRPM7 in the closed non-conducting state. Similar to other allosteric inhibitors of TRPM7, NS8593 and VER155008, binding of CCT is accompanied by displacement of a lipid that resides in the VL site in the apo condition. Moreover, we demonstrate the principal role of several residues in the VL site enabling CCT to inhibit TRPM7 without impacting the homologous TRPM6 channel. Hence, our results uncover the central role of the VL site for the selective interaction of TRPM7 with small molecules that can be explored in future drug design.
    MeSH term(s) TRPM Cation Channels/metabolism ; TRPM Cation Channels/antagonists & inhibitors ; Humans ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/chemistry ; Protein Serine-Threonine Kinases/metabolism ; Protein Serine-Threonine Kinases/antagonists & inhibitors ; HEK293 Cells ; Molecular Dynamics Simulation ; Binding Sites ; Protein Binding ; Cryoelectron Microscopy ; 1-Naphthylamine/analogs & derivatives
    Chemical Substances TRPM Cation Channels ; Antineoplastic Agents ; TRPM7 protein, human (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; (R)-N-(benzimidazol-2-yl)-1,2,3,4-tetrahydro-1-naphthylamine ; 1-Naphthylamine (9753I242R5)
    Language English
    Publishing date 2024-04-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2024.114108
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  6. Article ; Online: Mapping TRPM7 Function by NS8593

    Vladimir Chubanov / Thomas Gudermann

    International Journal of Molecular Sciences, Vol 21, Iss 7017, p

    2020  Volume 7017

    Abstract: The transient receptor potential cation channel, subfamily M, member 7 (TRPM7) is a ubiquitously expressed membrane protein, which forms a channel linked to a cytosolic protein kinase. Genetic inactivation of TRPM7 in animal models uncovered the critical ...

    Abstract The transient receptor potential cation channel, subfamily M, member 7 (TRPM7) is a ubiquitously expressed membrane protein, which forms a channel linked to a cytosolic protein kinase. Genetic inactivation of TRPM7 in animal models uncovered the critical role of TRPM7 in early embryonic development, immune responses, and the organismal balance of Zn 2+ , Mg 2+ , and Ca 2+ . TRPM7 emerged as a new therapeutic target because malfunctions of TRPM7 have been associated with anoxic neuronal death, tissue fibrosis, tumour progression, and giant platelet disorder. Recently, several laboratories have identified pharmacological compounds allowing to modulate either channel or kinase activity of TRPM7. Among other small molecules, NS8593 has been defined as a potent negative gating regulator of the TRPM7 channel. Consequently, several groups applied NS8593 to investigate cellular pathways regulated by TRPM7. Here, we summarize the progress in this research area. In particular, two notable milestones have been reached in the assessment of TRPM7 druggability. Firstly, several laboratories demonstrated that NS8593 treatment reliably mirrors prominent phenotypes of cells manipulated by genetic inactivation of TRPM7. Secondly, it has been shown that NS8593 allows us to probe the therapeutic potential of TRPM7 in animal models of human diseases. Collectively, these studies employing NS8593 may serve as a blueprint for the preclinical assessment of TRPM7-targeting drugs.
    Keywords TRPM7 ; NS8593 ; naltriben ; calcium ; magnesium ; zinc ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 572
    Language English
    Publishing date 2020-09-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Structural mechanisms of TRPM7 activation and inhibition.

    Nadezhdin, Kirill D / Correia, Leonor / Narangoda, Chamali / Patel, Dhilon S / Neuberger, Arthur / Gudermann, Thomas / Kurnikova, Maria G / Chubanov, Vladimir / Sobolevsky, Alexander I

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 2639

    Abstract: The transient receptor potential channel TRPM7 is a master regulator of the organismal balance of divalent cations that plays an essential role in embryonic development, immune responses, cell mobility, proliferation, and differentiation. TRPM7 is ... ...

    Abstract The transient receptor potential channel TRPM7 is a master regulator of the organismal balance of divalent cations that plays an essential role in embryonic development, immune responses, cell mobility, proliferation, and differentiation. TRPM7 is implicated in neuronal and cardiovascular disorders, tumor progression and has emerged as a new drug target. Here we use cryo-EM, functional analysis, and molecular dynamics simulations to uncover two distinct structural mechanisms of TRPM7 activation by a gain-of-function mutation and by the agonist naltriben, which show different conformational dynamics and domain involvement. We identify a binding site for highly potent and selective inhibitors and show that they act by stabilizing the TRPM7 closed state. The discovered structural mechanisms provide foundations for understanding the molecular basis of TRPM7 channelopathies and drug development.
    MeSH term(s) TRPM Cation Channels/metabolism ; Cell Differentiation
    Chemical Substances TRPM Cation Channels
    Language English
    Publishing date 2023-05-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-38362-3
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  8. Article ; Online: TRPM7 reflected in Cryo-EMirror.

    Chubanov, Vladimir / Mittermeier, Lorenz / Gudermann, Thomas

    Cell calcium

    2018  Volume 76, Page(s) 129–131

    Abstract: TRPM7 is an atypical type of ion channel because its pore-forming moiety is covalently linked to a protein kinase domain. The channel-kinase TRPM7 controls a wide range of biological processes such as mineral homeostasis, immune responses, cell motility, ...

    Abstract TRPM7 is an atypical type of ion channel because its pore-forming moiety is covalently linked to a protein kinase domain. The channel-kinase TRPM7 controls a wide range of biological processes such as mineral homeostasis, immune responses, cell motility, proliferation and differentiation. Earlier this year, Duan J & co-workers [1] published three TRPM7 structures resolved by cryo-electron microscopy (cryo-EM). This study tremendously advances our mechanistic understanding of TRPM7 channel function and forms the basis for informed structure-function assessment of this extraordinary protein.
    MeSH term(s) Animals ; Calcium ; Cryoelectron Microscopy ; Homeostasis ; Humans ; Magnesium ; Protein-Serine-Threonine Kinases ; TRPM Cation Channels
    Chemical Substances TRPM Cation Channels ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; TRPM7 protein, human (EC 2.7.11.1) ; Magnesium (I38ZP9992A) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2018-11-15
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 757687-0
    ISSN 1532-1991 ; 0143-4160
    ISSN (online) 1532-1991
    ISSN 0143-4160
    DOI 10.1016/j.ceca.2018.11.004
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  9. Article ; Online: Pharmacological agents selectively acting on the channel moieties of TRPM6 and TRPM7.

    Rössig, Anna / Hill, Kerstin / Nörenberg, Wolfgang / Weidenbach, Sebastian / Zierler, Susanna / Schaefer, Michael / Gudermann, Thomas / Chubanov, Vladimir

    Cell calcium

    2022  Volume 106, Page(s) 102640

    Abstract: The transient receptor potential cation channel, subfamily M, members 6 and 7 (TRPM6 and TRPM7) are homologous membrane proteins encompassing cation channel units fused to cytosolic serine/threonine-protein kinase domains. Clinical studies and ... ...

    Abstract The transient receptor potential cation channel, subfamily M, members 6 and 7 (TRPM6 and TRPM7) are homologous membrane proteins encompassing cation channel units fused to cytosolic serine/threonine-protein kinase domains. Clinical studies and experiments with animal disease models suggested that selective inhibition of TRPM6 and TRPM7 currents might be beneficial for subjects with immune and cardiovascular disorders, tumours and other pathologies, but the suitable pharmacological toolkit remains underdeveloped. The present study identified small synthetic molecules acting specifically on the channel moieties of TRPM6 and TRPM7. Using electrophysiological analysis in conjunction with Ca
    MeSH term(s) Animals ; Humans ; Isoxazoles/pharmacology ; Magnesium/metabolism ; Mice ; Piperidines/pharmacology ; Protein Serine-Threonine Kinases ; Purine Nucleosides/pharmacology ; TRPM Cation Channels/drug effects ; TRPM Cation Channels/metabolism ; Transient Receptor Potential Channels/drug effects ; Transient Receptor Potential Channels/metabolism
    Chemical Substances Isoxazoles ; Piperidines ; Purine Nucleosides ; TRPM Cation Channels ; TRPM6 protein, human ; Transient Receptor Potential Channels ; Trpm6 protein, mouse ; VER 155008 ; 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) ; iloperidone (VPO7KJ050N)
    Language English
    Publishing date 2022-08-17
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 757687-0
    ISSN 1532-1991 ; 0143-4160
    ISSN (online) 1532-1991
    ISSN 0143-4160
    DOI 10.1016/j.ceca.2022.102640
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  10. Article ; Online: Assessment of TRPM7 functions by drug-like small molecules.

    Chubanov, Vladimir / Ferioli, Silvia / Gudermann, Thomas

    Cell calcium

    2017  Volume 67, Page(s) 166–173

    Abstract: Transient receptor potential cation channel subfamily M member 7 (TRPM7) is a plasma membrane ion channel linked to a cytosolic protein kinase domain. Genetic inactivation of this bi-functional protein revealed its crucial role in ... ...

    Abstract Transient receptor potential cation channel subfamily M member 7 (TRPM7) is a plasma membrane ion channel linked to a cytosolic protein kinase domain. Genetic inactivation of this bi-functional protein revealed its crucial role in Ca
    Language English
    Publishing date 2017-11
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 757687-0
    ISSN 1532-1991 ; 0143-4160
    ISSN (online) 1532-1991
    ISSN 0143-4160
    DOI 10.1016/j.ceca.2017.03.004
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