The Mg2+ and Mg2+-Nucleotide-Regulated Channel-Kinase TRPM7

Penner, Reinhold; Fleig, Andrea

doi:10.1007/978-3-540-34891-7_19

Cited by 96 publications

(87 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Schweyen and colleagues (7,47,180) studied Mrs2 amino acid structure to determine the relationship of group II intron splicing with changes in Mrs2 transport, inasmuch as both functions are associated. Because Mrs2 shares some amino acid sequences with bacterial CorA, the availability of the crystal structure of CorA may be informative in describing Mg 2ϩ movement through the mammalian Mrs2 protein (87,105 (107,127,156). TRPM proteins possess six predicted TMs.…”

Section: Mammalian Mg 2؉ Transportersmentioning

confidence: 99%

“…Hydrophobic regions between TM5 and TM6 are thought to contribute to the cation pore when four channel subunits coalesce to form the functional transporter (16). Unlike other members of the TRPM channel superfamily, the homologs TRPM6 and TRPM7 possess a COOH terminus, Thr/Ser kinase, that belongs to an atypical family of eukaryotic ␣-kinases (107,127). According, these proteins are termed "chanzymes."…”

Section: Mammalian Mg 2؉ Transportersmentioning

confidence: 99%

See 1 more Smart Citation

Molecular identification of ancient and modern mammalian magnesium transporters

Quamme

2010

American Journal of Physiology-Cell Physiology

172

182

View full text Add to dashboard Cite

handling is poorly understood.The purpose of this review is to describe some of the recent insights into the identification and function of mammalian Mg 2ϩ transporters. There is a large body of physiological evidence for mammalian Mg 2ϩ transporters, which have only begun to be identified on the molecular level (11, 51,109,117,135,148,170). In particular, I will detail, at some length, the novel Mg 2ϩ transporters that have been identified over the last several years. These will be examined from the perspective of the established and more characterized mammalian Mg 2ϩ channels, mitochondrial Mrs2 and TRPM7/6. I will briefly review plant, bacterial, and yeast transporters as they relate to our newly identified mammalian Mg 2ϩ transporters, because some of these proteins share characteristics with the more ancient forms of transporters. The identification and characterization of plant, prokaryote, and yeast Mg 2ϩ transporters have been extensively reviewed elsewhere (35, 70, 73, 138).

show abstract

Section: Mammalian Mg 2؉ Transportersmentioning

confidence: 99%

Section: Mammalian Mg 2؉ Transportersmentioning

confidence: 99%

Molecular identification of ancient and modern mammalian magnesium transporters

Quamme

2010

American Journal of Physiology-Cell Physiology

172

182

View full text Add to dashboard Cite

show abstract

“…Other aspects of TRPM channels are addressed in a number of excellent review articles. 7,12,[57][58][59][60][61][62][63][64] A few years ago, two independent groups showed that loss-of-function mutations in the human TRPM6 gene are the molecular cause of HSH. 10,56 HSH is an autosomal recessive disease that manifests in early infancy with generalized convulsions or symptoms of increased neuromuscular excitability including muscle spasms and tet-any.…”

Section: Role Of Trpm6 Channels In Renal Magnesium Homeostasismentioning

confidence: 99%

Renal TRPathies

Dietrich¹,

Chubanov²,

Gudermann³

2010

Journal of the American Society of Nephrology

View full text Add to dashboard Cite

One key function of the kidneys is the ultrafiltration of plasma by glomeruli to dispose of metabolic end products, excess electrolytes, and water. A vast array of ion channels and transporters are critical for filtration, secretion, and resorption of electrolytes to maintain homeostasis. In recent years, investigations have focused on several members of the large transient receptor potential (TRP) family of ion channels, because mutations in genes encoding members of three different TRP ion channel subfamilies have been linked to human kidney diseases. 1 Mutations in PKD1 (encoding TRPP1) and PKD2 (coding for TRPP2) occur at high frequency in individuals with autosomal dominant polycystic kidney disease. 2,3 The latter mutations and the pathophysiology of polycystic kidney disease are not discussed further in this overview because the topic has been covered by numerous insightful review articles. 4 -7 Missense and nonsense mutations in the gene coding for TRPC6 segregate with autosomal dominant FSGS, a kidney disease that leads to progressive renal failure. 8,9 Loss-of-function mutations in TRPM6 are also associated with hypomagnesemia with secondary hypocalcemia (HSH), a rare autosomal recessive disorder. 10 -12 The involvement of TRP channel mutations in hereditary kidney disease has shed new light on the molecular pathogenesis of renal failure and significantly enhanced our appreciation of the physiologic roles of TRP channels on tubular function. In this review, we focus exclusively on TRPC6 and TRPM6. TRPC6 AND PODOCYTE FUNCTIONTRPC6 is a nonselective cation channel and one of the seven members of the classical transient receptor potential (TRPC) family, which can be divided into subfamilies on the basis of amino acid similarity. Whereas TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approximately 64% amino acid identity. TRPC3, TRPC6, and TRPC7 form a structural and functional subfamily displaying 65 to 78% identity at the amino acid level and share a common activator, diacylglycerol (DAG). 13 DAG is produced by phospholipase C isozymes activated after agonist binding to appropriate receptors, such as the interaction of angiotensin II (AngII) with AT 1 receptors.Like all TRPC family members, TRPC6 harbors an invariant sequence, the TRP box (containing the amino acid sequence EWKFAR), in its C-terminal tail as well as three ankyrin repeats in the N-terminus (Figure 1, A and B). The predicted transmembrane topology is similar to that of other TRP channels with intracellular N-and C-termini, six membrane-spanning helices (S1 through S6), and a presumed pore-forming loop (P) between S5 and S6 (Figure 1, A and B). As deduced from Northern blot analyses, TRPC6 channels are most prominently expressed in lung tissues, 14 where they ABSTRACTMany ion channels and transporters are involved in the filtration, secretion, and resorption of electrolytes by the kidney. In recent years, the superfamily of transient receptor potential (TRP) ion channels have received deserved attention because mutated TRP ch...

show abstract

“…Mechanical stress such as membrane stretch or osmotic cell swelling can activate TRPM7--like channels (Numata et al, 2007), which are involved in Mg transport. These channels are members of the ubiquitously expressed melastatin--related subfamily of transient receptor potential (TRP) channels, and represent essential mediators of anoxic neuronal death Penner and Fleig, 2007). Low intracellular levels of Mg, a process that exacerbates the effects of stress on the organism, also activate TRPM7 channels.…”

Section: Neurological Function Of Magnesiummentioning

confidence: 99%

Magnesium in the Central Nervous System

Turner

Vink

New Perspectives in Magnesium Research

View full text Add to dashboard Cite

The Mg2+ and Mg2+-Nucleotide-Regulated Channel-Kinase TRPM7

Cited by 96 publications

References 45 publications

Molecular identification of ancient and modern mammalian magnesium transporters

Molecular identification of ancient and modern mammalian magnesium transporters

Renal TRPathies

Magnesium in the Central Nervous System

Contact Info

Product

Resources

About