TRPM7

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TRPM7
Protein TRPM7 PDB 1ia9.png
Identifiers
Aliases TRPM7, ALSPDC, CHAK, CHAK1, LTRPC7, LTrpC-7, TRP-PLIK, transient receptor potential cation channel subfamily M member 7
External IDs OMIM: 605692 MGI: 1929996 HomoloGene: 9774 GeneCards: TRPM7
Targeted by Drug
adenosine cyclic phosphate, adenosine triphosphate, Hydron, nafamostat[1]
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001301212
NM_017672

NM_001164325
NM_021450

RefSeq (protein)

NP_001288141
NP_060142

NP_001157797.1
NP_067425.2
NP_001157797
NP_067425

Location (UCSC) Chr 15: 50.55 – 50.69 Mb Chr 2: 126.79 – 126.88 Mb
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Transient receptor potential cation channel, subfamily M, member 7, also known as TRPM7, is a human gene encoding a protein of the same name.

Function[edit]

TRPs, mammalian homologs of the Drosophila transient receptor potential (trp) protein, are ion channels that are thought to mediate capacitative calcium entry into the cell. TRP-PLIK is a protein that is both an ion channel and a kinase. As a channel, it conducts calcium and monovalent cations to depolarize cells and increase intracellular calcium. As a kinase, it is capable of phosphorylating itself and other substrates. The kinase activity is necessary for channel function, as shown by its dependence on intracellular ATP and by the kinase mutants.[supplied by OMIM][4]

Interactions[edit]

TRPM7 has been shown to interact with PLCB1[5] and PLCB2.[5]

Clinical relevance[edit]

Defects in this gene have been associated to magnesium deficiency in human microvascular endothelial cells.[6]

See also[edit]

References[edit]

  1. ^ "Drugs that physically interact with Transient receptor potential cation channel subfamily M member 7 view/edit references on wikidata". 
  2. ^ "Human PubMed Reference:". 
  3. ^ "Mouse PubMed Reference:". 
  4. ^ "Entrez Gene: TRPM7 transient receptor potential cation channel, subfamily M, member 7". 
  5. ^ a b Runnels LW, Yue L, Clapham DE (May 2002). "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. doi:10.1038/ncb781. PMID 11941371. 
  6. ^ Baldoli E, Maier JA (20 December 2011). "Silencing TRPM7 mimics the effects of magnesium deficiency in human microvascular endothelial cells". Angiogenesis. 15 (1): 47–57. doi:10.1007/s10456-011-9242-0. PMID 22183257.  Check date values in: |year= / |date= mismatch (help)

Further reading[edit]

  • Chubanov V, Gudermann T, Schlingmann KP (2005). "Essential role for TRPM6 in epithelial magnesium transport and body magnesium homeostasis". Pflugers Arch. 451 (1): 228–34. doi:10.1007/s00424-005-1470-y. PMID 16075242. 
  • Clapham DE, Julius D, Montell C, Schultz G (2005). "International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels". Pharmacol. Rev. 57 (4): 427–50. doi:10.1124/pr.57.4.6. PMID 16382100. 
  • Penner R, Fleig A (2007). "The Mg2+ and Mg(2+)-nucleotide-regulated channel-kinase TRPM7". Handb Exp Pharmacol. 179 (179): 313–28. doi:10.1007/978-3-540-34891-7_19. PMID 17217066. 

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.