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TRPM7

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Identifiers
SymbolsTRPM7 ; ALSPDC; CHAK; CHAK1; LTRPC7; LTrpC-7; TRP-PLIK
External IDsOMIM605692 HomoloGene9774 IUPHAR: 499 ChEMBL: 1250412 GeneCards: TRPM7 Gene
EC number2.7.11.1
Orthologs
SpeciesHumanMouse
Entrez5482258800
EnsemblENSG00000092439ENSMUSG00000027365
UniProtQ96QT4Q923J1
RefSeq (mRNA)NM_001301212NM_001164325
RefSeq (protein)NP_001288141NP_001157797
Location (UCSC)Chr 15:
50.84 – 50.98 Mb
Chr 2:
126.79 – 126.88 Mb
PubMed search[1][2]

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

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][1]

Interactions

TRPM7 has been shown to interact with PLCB1[2] and PLCB2.[2]

Clinical relevance

Defects in this gene have been associated to magnesium deficiency in human microvascular endothelial cells.[3]

See also

References

  1. ^ "Entrez Gene: TRPM7 transient receptor potential cation channel, subfamily M, member 7". 
  2. ^ 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. PMID 11941371. doi:10.1038/ncb781. 
  3. ^ 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. PMID 22183257. doi:10.1007/s10456-011-9242-0.  Check date values in: |year= / |date= mismatch (help)

Further reading

  • 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. PMID 16075242. doi:10.1007/s00424-005-1470-y. 
  • 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. PMID 16382100. doi:10.1124/pr.57.4.6. 
  • Penner R, Fleig A (2007). "The Mg2+ and Mg(2+)-nucleotide-regulated channel-kinase TRPM7". Handb Exp Pharmacol 179 (179): 313–28. PMID 17217066. doi:10.1007/978-3-540-34891-7_19. 
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External links

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

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