TRPM6: A Janus-like protein.
TRPM6 and TRPM7 proteins share similar molecular structures and biophysical properties. Both proteins are Mg(2+)- and Ca(2+)-permeable cation channels with the typical topology of six transmembrane domains. In addition, TRPM6 and TRPM7 function as serine/threonine kinases with kinase domains at their C-terminal tails. At present, the role of the association of kinase and channel domains in TRPM6 and TRPM7 remains elusive. TRPM6 is mainly expressed in kidney and intestine, where it might be responsible for epithelial Mg2+ re/absorption. This hypothesis is strengthened by the identification of TRPM6 mutants in patients with a rare but severe hereditary disease called hypomagnesaemia with secondary hypocalcaemia. The aim of this review is to provide a brief but concise overview of the information currently available about TRPM6.
Bödding
M
M
Experimentelle und Klinische Pharmakologie und Toxikologie, Universität des Saarlandes, 66421 Homburg, Germany. matthias.boedding@uniklinik-saarland.de
D000818:Animals; D001711:Biotransformation / Q000187:drug effects; D006801:Humans; D007473:Ion Channels / Q000378:metabolism / Q000502:physiology; D010770:Phosphotransferases / Q000378:metabolism; D050053:TRPM Cation Channels / Q000737:chemistry / Q000187:drug effects* / Q000235:genetics* / Q000378:metabolism / Q000502:physiology*; D014018:Tissue Distribution
D007473:Ion Channels; D050053:TRPM Cation Channels; C459082:TRPM6 protein, human; C507531:TRPM6 protein, rat; D010770:Phosphotransferases