Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2004-3-3
pubmed:databankReference
pubmed:abstractText
Impaired magnesium reabsorption in patients with TRPM6 gene mutations stresses an important role of TRPM6 (melastatin-related TRP cation channel) in epithelial magnesium transport. While attempting to isolate full-length TRPM6, we found that the human TRPM6 gene encodes multiple mRNA isoforms. Full-length TRPM6 variants failed to form functional channel complexes because they were retained intracellularly on heterologous expression in HEK 293 cells and Xenopus oocytes. However, TRPM6 specifically interacted with its closest homolog, the Mg(2+)-permeable cation channel TRPM7, resulting in the assembly of functional TRPM6/TRPM7 complexes at the cell surface. The naturally occurring S141L TRPM6 missense mutation abrogated the oligomeric assembly of TRPM6, thus providing a cell biological explanation for the human disease. Together, our data suggest an important contribution of TRPM6/TRPM7 heterooligomerization for the biological role of TRPM6 in epithelial magnesium absorption.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-10922295, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-11007484, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-11152754, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-11161216, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-11357414, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-11385574, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-11401515, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-11707492, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-11713258, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-11891065, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-11941371, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-12032305, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-12032568, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-12032570, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-12377790, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-12508053, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-12574114, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-12647029, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-12651871, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-12842017, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-12887921, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-14576148, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-14654832, http://linkedlifedata.com/resource/pubmed/commentcorrection/14976260-14657417
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
101
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2894-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:14976260-Animals, pubmed-meshheading:14976260-Biological Transport, pubmed-meshheading:14976260-Cell Line, pubmed-meshheading:14976260-Cell Membrane, pubmed-meshheading:14976260-Cloning, Molecular, pubmed-meshheading:14976260-Female, pubmed-meshheading:14976260-Humans, pubmed-meshheading:14976260-Hypocalcemia, pubmed-meshheading:14976260-Ion Channels, pubmed-meshheading:14976260-Kinetics, pubmed-meshheading:14976260-Magnesium Deficiency, pubmed-meshheading:14976260-Manganese, pubmed-meshheading:14976260-Membrane Potentials, pubmed-meshheading:14976260-Membrane Proteins, pubmed-meshheading:14976260-Molecular Sequence Data, pubmed-meshheading:14976260-Mutation, pubmed-meshheading:14976260-Oocytes, pubmed-meshheading:14976260-Protein Kinases, pubmed-meshheading:14976260-Recombinant Proteins, pubmed-meshheading:14976260-TRPM Cation Channels, pubmed-meshheading:14976260-Xenopus laevis
pubmed:year
2004
pubmed:articleTitle
Disruption of TRPM6/TRPM7 complex formation by a mutation in the TRPM6 gene causes hypomagnesemia with secondary hypocalcemia.
pubmed:affiliation
Institute for Pharmacology and Toxicology, Philipps University Marburg, 35033 Marburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't