Molecular determinants of Mg2+ and Ca2+ permeability and pH sensitivity in TRPM6 and TRPM7
The channel kinases TRPM6 and TRPM7 have recently been discovered to play important
roles in Mg 2+ and Ca 2+ homeostasis, which is critical to both human health and cell …
roles in Mg 2+ and Ca 2+ homeostasis, which is critical to both human health and cell …
Alternative splicing switches the divalent cation selectivity of TRPM3 channels
J Oberwinkler, A Lis, KM Giehl, V Flockerzi… - Journal of Biological …, 2005 - ASBMB
TRPM3 is a poorly understood member of the large family of transient receptor potential
(TRP) ion channels. Here we describe five novel splice variants of TRPM3, TRPM3α1–5 …
(TRP) ion channels. Here we describe five novel splice variants of TRPM3, TRPM3α1–5 …
The selectivity filter of the cation channel TRPM4
B Nilius, J Prenen, A Janssens, G Owsianik… - Journal of Biological …, 2005 - ASBMB
Transient receptor potential channel melastatin subfamily (TRPM) 4 and its close
homologue, TRPM5, are the only two members of the large transient receptor potential …
homologue, TRPM5, are the only two members of the large transient receptor potential …
Functional characterization of homo-and heteromeric channel kinases TRPM6 and TRPM7
M Li, J Jiang, L Yue - The Journal of general physiology, 2006 - rupress.org
TRPM6 and TRPM7 are two known channel kinases that play important roles in various
physiological processes, including Mg2+ homeostasis. Mutations in TRPM6 cause …
physiological processes, including Mg2+ homeostasis. Mutations in TRPM6 cause …
TRPM6 and TRPM7 differentially contribute to the relief of heteromeric TRPM6/7 channels from inhibition by cytosolic Mg2+ and Mg·ATP
S Ferioli, S Zierler, J Zaißerer, J Schredelseker… - Scientific reports, 2017 - nature.com
TRPM6 and its homologue TRPM7 are α-kinase-coupled divalent cation-selective channels
activated upon reduction of cytosolic levels of Mg2+ and Mg· ATP. TRPM6 is vital for …
activated upon reduction of cytosolic levels of Mg2+ and Mg· ATP. TRPM6 is vital for …
Structural mechanism of TRPM7 channel regulation by intracellular magnesium
E Schmidt, C Narangoda, W Nörenberg… - Cellular and Molecular …, 2022 - Springer
Abstract Zn2+, Mg2+ and Ca2+ are essential divalent cations implicated in many metabolic
processes and signalling pathways. An emerging new paradigm is that the organismal …
processes and signalling pathways. An emerging new paradigm is that the organismal …
TRPM7 channel is regulated by magnesium nucleotides via its kinase domain
P Demeuse, R Penner, A Fleig - The Journal of general physiology, 2006 - rupress.org
TRPM7 is a Ca2+-and Mg2+-permeable cation channel that also contains a protein kinase
domain. While there is general consensus that the channel is inhibited by free intracellular …
domain. While there is general consensus that the channel is inhibited by free intracellular …
Evolutionary determinants of divergent calcium selectivity of TRPM channels
MM Schnitzler, J Wäring, T Gudermann… - The FASEB …, 2008 - Wiley Online Library
The mammalian TRPM gene family can be subdivided into distinct categories of cation chan
nels that are either highly permeable for Ca2+ (TRPM3/6/7), nonselective (TRPM2/8), or …
nels that are either highly permeable for Ca2+ (TRPM3/6/7), nonselective (TRPM2/8), or …
The channel kinases TRPM6 and TRPM7 are functionally nonredundant
C Schmitz, MV Dorovkov, X Zhao, BJ Davenport… - Journal of Biological …, 2005 - ASBMB
TRPM7 and its closest homologue, TRPM6, are the only known fusions of an ion channel
pore with a kinase domain. Deletion of TRPM7 in DT40 B-lymphocytes causes growth arrest …
pore with a kinase domain. Deletion of TRPM7 in DT40 B-lymphocytes causes growth arrest …
Trpm7
A Fleig, V Chubanov - … Receptor Potential (TRP) Cation Channels: Volume …, 2014 - Springer
The channel kinases TRPM6 and TRPM7 are fusion proteins with an ion transport domain
and an enzymatically active kinase domain. TRPM7 has been found in every mammalian …
and an enzymatically active kinase domain. TRPM7 has been found in every mammalian …