TRPs, mammalian homologs of the Drosophilatransient 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]
^ abRunnels 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. PMID11941371.
^Baldoli E, Maier JA (20 December 2011). "Silencing TRPM7 mimics the effects of magnesium deficiency in human microvascular endothelial cells". Angiogenesis15 (1): 47–57. doi:10.1007/s10456-011-9242-0. PMID22183257.Check date values in: |year= / |date= mismatch (help)
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. PMID16075242.
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. PMID16382100.