TRPM7: Difference between revisions

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== Clinical relevance ==
== Clinical relevance ==


Defects in this gene have been associated to magnesium deficiency in human microvascular endothelial cells.<ref name="doi.10.1007/s10456-011-9242-0">{{cite journal | vauthors = Baldoli E, Maier JA | title = Silencing TRPM7 mimics the effects of magnesium deficiency in human microvascular endothelial cells | journal = Angiogenesis | volume = 15 | issue = 1 | pages = 47–57 | year = 2012 | date = 20 December 2011 | pmid = 22183257 | doi = 10.1007/s10456-011-9242-0 }}</ref>
Defects in this gene have been associated to magnesium deficiency in human microvascular endothelial cells.<ref name="doi.10.1007/s10456-011-9242-0">{{cite journal | vauthors = Baldoli E, Maier JA | title = Silencing TRPM7 mimics the effects of magnesium deficiency in human microvascular endothelial cells | journal = Angiogenesis | volume = 15 | issue = 1 | pages = 47–57 | year = 2012 | pmid = 22183257 | doi = 10.1007/s10456-011-9242-0 }}</ref>


== See also ==
== See also ==
Line 22: Line 22:
== Further reading ==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
* {{cite journal | vauthors = Chubanov V, Gudermann T, Schlingmann KP | title = Essential role for TRPM6 in epithelial magnesium transport and body magnesium homeostasis | journal = Pflugers Arch. | volume = 451 | issue = 1 | pages = 228–34 | year = 2005 | pmid = 16075242 | doi = 10.1007/s00424-005-1470-y }}
* {{cite journal | vauthors = Chubanov V, Gudermann T, Schlingmann KP | title = Essential role for TRPM6 in epithelial magnesium transport and body magnesium homeostasis | journal = Pflügers Arch. | volume = 451 | issue = 1 | pages = 228–34 | year = 2005 | pmid = 16075242 | doi = 10.1007/s00424-005-1470-y }}
* {{cite journal | vauthors = Clapham DE, Julius D, Montell C, Schultz G | title = International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels | journal = Pharmacol. Rev. | volume = 57 | issue = 4 | pages = 427–50 | year = 2005 | pmid = 16382100 | doi = 10.1124/pr.57.4.6 }}
* {{cite journal | vauthors = Clapham DE, Julius D, Montell C, Schultz G | title = International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels | journal = Pharmacol. Rev. | volume = 57 | issue = 4 | pages = 427–50 | year = 2005 | pmid = 16382100 | doi = 10.1124/pr.57.4.6 }}
* {{cite journal | vauthors = Penner R, Fleig A | title = The Mg2+ and Mg(2+)-nucleotide-regulated channel-kinase TRPM7 | journal = Handb Exp Pharmacol | volume = 179 | issue = 179 | pages = 313–28 | year = 2007 | pmid = 17217066 | doi = 10.1007/978-3-540-34891-7_19 }}
* {{cite journal | vauthors = Penner R, Fleig A | title = The Mg2+ and Mg(2+)-nucleotide-regulated channel-kinase TRPM7 | journal = Handb Exp Pharmacol | volume = 179 | issue = 179 | pages = 313–28 | year = 2007 | pmid = 17217066 | doi = 10.1007/978-3-540-34891-7_19 }}

Latest revision as of 12:40, 9 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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Wikidata
View/Edit Human

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. ↑ 2.0 2.1 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.
  3. ↑ Baldoli E, Maier JA (2012). "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.

Further reading

  • Chubanov V, Gudermann T, Schlingmann KP (2005). "Essential role for TRPM6 in epithelial magnesium transport and body magnesium homeostasis". Pflügers 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

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


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