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From Wikipedia, the free encyclopedia

TRPM is a family of transient receptor potential ion channels (the "M" stands for "melastatin").[1] Functional TRPM channels are believed to form tetramers.[2]

Unlike the TRPC and TRPV sub-families, TRPM subunits do not contain N-terminal ankyrin repeat motifs but, rather, contain entire functional proteins in their C-termini. TRPM6 and TRPM7, for example, contain functional α-kinase segments, which are a type of serine/threonine-specific protein kinase.

Contents

Permeability and activation

The relative permeability of calcium and magnesium varies widely among TRPM channels.

The mechanism of activation also varies greatly among TRPM channels.

  • TRPM2 is activated by ADP-ribose Adenosine 5'-diphosphoribose and functions as a sensor of redox status in cells.[3]
  • TRPM4 and TRPM5 are activated by intracellular calcium.
  • TRPM8, conversely, can be activated by low temperatures, menthol, eucalyptol and icilin.[4][5]

Functions

Among the functional responsibilities of the TRPM channels are:

  • regulation of calcium oscillations after T cell activation (TRPM4).[6]
  • sensory transduction in taste cells (TRPM5).
  • cold sensation (TRPM8)
  • regulation of magnesium reabsorption in the kidneys and absorption in the intestines (TRPM6).[7]
  • regulation of cell adhesion (TRPM7).[8]

Genes

References

  1. ^ Kraft R, Harteneck C (2005). "The mammalian melastatin-related transient receptor potential cation channels: an overview". Pflugers Arch 451 (1): 204–11. doi:10.1007/s00424-005-1428-0. PMID 15895246.  
  2. ^ Jiang LH (2007). "Subunit interaction in channel assembly and functional regulation of transient receptor potential melastatin (TRPM) channels". Biochem Soc Trans 35 (1): 86–8. doi:10.1042/BST0350086. PMID 17233608.  
  3. ^ Hara Y, Wakamori M, Ishii M, Maeno E, Nishida M, Yoshida T, Yamada H, Shimizu S, Mori E, Kudoh J, Shimizu N, Kurose H, Okada Y, Imoto K, Mori Y (2002). "LTRPC2 Ca2+-permeable channel activated by changes in redox status confers susceptibility to cell death". Mol Cell 9 (1): 163–73. doi:10.1016/S1097-2765(01)00438-5. PMID 11804595.  
  4. ^ Behrendt HJ, Germann T, Gillen C, Hatt H, Jostock R (2004). "Characterization of the mouse cold-menthol receptor TRPM8 and vanilloid receptor type-1 VR1 using a fluorometric imaging plate reader (FLIPR) assay". Br. J. Pharmacol. 141 (4): 737–45. doi:10.1038/sj.bjp.0705652. PMID 14757700.  
  5. ^ Nilius B, Owsianik G, Voets T, Peters JA (2007). "Transient receptor potential cation channels in disease". Physiol. Rev. 87 (1): 165–217. doi:10.1152/physrev.00021.2006. PMID 17237345.  
  6. ^ Launay P, Cheng H, Srivatsan S, Penner R, Fleig A, Kinet J.-P. (2004). "TRPM4 regulates calcium oscillations after T cell activation". Science 306: 1374–77. doi:10.1126/science.1098845. PMID 15550671.  
  7. ^ Schlingmann KP, Weber S, Peters M, Niemann Nejsum L, Vitzthum H, Klingel K, Kratz M, Haddad E, Ristoff E, Dinour D, Syrrou M, Nielsen S, Sassen M, Waldegger S, Seyberth HW, Konrad M (2002). "Hypomagnesemia with secondary hypocalcemia is caused by mutations in TRPM6, a new member of the TRPM gene family". Nat. Genet. 31 (2): 166–70. doi:10.1038/ng889. PMID 12032568.  
  8. ^ Su L-T., Agapito MA, Li M, Simonson WTN, Huttenlocher A, Habas R, Yue L, Runnels LW (2006). "TRPM7 regulates cell adhesion by controlling the calcium-dependent protease calpain". J. Biol. Chem. 281 (16): 11260–70. doi:10.1074/jbc.M512885200. PMID 16436382.  

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