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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Flockerzi, Veit Zhu, Michael X. Sell, Thomas Speicher, Tilman Stoerger, Christof Wissenbach, Ulrich Cavalié, Adolfo Helms, Volkhard Abdulmughni, Ammar Jusoh, Siti A. Philipp, Stephan E. Beck, Andreas Dettmer, Viviane |
| Description | Author Affiliation: Beck A ( Experimentelle und Klinische Pharmakologie und Toxikologie, Universität des Saarlandes, 66421 Homburg, Germany. andreas.beck@uniklinikum-saarland.de) |
| Abstract | TRPC4 and TRPC5 proteins share 65% amino acid sequence identity and form Ca(2+)-permeable nonselective cation channels. They are activated by stimulation of receptors coupled to the phosphoinositide signaling cascade. Replacing a conserved glycine residue within the cytosolic S4-S5 linker of both proteins by a serine residue forces the channels into an open conformation. Expression of the TRPC4G503S and TRPC5G504S mutants causes cell death, which could be prevented by buffering the Ca(2+) of the culture medium. Current-voltage relationships of the TRPC4G503S and TRPC5G504S mutant ion channels resemble that of fully activated TRPC4 and TRPC5 wild-type channels, respectively. Modeling the structure of the transmembrane domains and the pore region (S4-S6) of TRPC4 predicts a conserved serine residue within the C-terminal sequence of the predicted S6 helix as a potential interaction site. Introduction of a second mutation (S623A) into TRPC4G503S suppressed the constitutive activation and partially rescued its function. These results indicate that the S4-S5 linker is a critical constituent of TRPC4/C5 channel gating and that disturbance of its sequence allows channel opening independent of any sensor domain. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 27 |
| Volume Number | 288 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2013-07-05 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Ion Channel Gating Physiology TRPC Cation Channels Metabolism Amino Acid Substitution Animals HEK293 Cells Mice Models, Molecular Mutation, Missense Peptide Mapping Protein Structure, Secondary Protein Structure, Tertiary Genetics Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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