TRPM7

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Transient receptor potential cation channel, subfamily M, member 7
Protein TRPM7 PDB 1ia9.png
PDB rendering based on 1ia9.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols TRPM7 ; ALSPDC; CHAK; CHAK1; LTRPC7; LTrpC-7; TRP-PLIK
External IDs OMIM605692 HomoloGene9774 IUPHAR: TRPM7 ChEMBL: 1250412 GeneCards: TRPM7 Gene
EC number 2.7.11.1
Orthologs
Species Human Mouse
Entrez 54822 58800
Ensembl ENSG00000092439 ENSMUSG00000027365
UniProt Q96QT4 Q923J1
RefSeq (mRNA) NM_001301212 NM_001164325
RefSeq (protein) NP_001288141 NP_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[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][1]

See also[edit]

Interactions[edit]

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

Clinical relevance[edit]

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

References[edit]

  1. ^ "Entrez Gene: TRPM7 transient receptor potential cation channel, subfamily M, member 7". 
  2. ^ a b Runnels, Loren W; Yue Lixia; Clapham David E (May 2002). "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. (England) 4 (5): 329–36. doi:10.1038/ncb781. ISSN 1465-7392. PMID 11941371. 
  3. ^ Baldoli, Erika; Maier, Jeanette A. M. (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. 

Further reading[edit]

  • Chubanov V, Gudermann T, Schlingmann KP (2006). "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 (2006). "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.