Conserved gating elements in TRPC4 and TRPC5 channels
TRPC4 and TRPC5 proteins share 65% amino acid sequence identity and form Ca2+-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 prot...
Main Authors: | , , , , , , , , , , , , |
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Format: | Article |
Language: | English |
Subjects: | |
Online Access: | View Fulltext in Publisher View in Scopus |
LEADER | 04186nam a2200937Ia 4500 | ||
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001 | 10.1074-jbc.M113.478305 | ||
008 | 220112s2013 CNT 000 0 und d | ||
020 | |a 00219258 (ISSN) | ||
245 | 1 | 0 | |a Conserved gating elements in TRPC4 and TRPC5 channels |
856 | |z View Fulltext in Publisher |u https://doi.org/10.1074/jbc.M113.478305 | ||
856 | |z View in Scopus |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-84880072077&doi=10.1074%2fjbc.M113.478305&partnerID=40&md5=b8fe7638c740d78199aa4a03e1cd0988 | ||
520 | 3 | |a TRPC4 and TRPC5 proteins share 65% amino acid sequence identity and form Ca2+-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 Ca2+ 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. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. | |
650 | 0 | 4 | |a Activation analysis |
650 | 0 | 4 | |a Amino acid sequence |
650 | 0 | 4 | |a Amino Acid Substitution |
650 | 0 | 4 | |a Amino acids |
650 | 0 | 4 | |a Animals |
650 | 0 | 4 | |a article |
650 | 0 | 4 | |a biotinylation |
650 | 0 | 4 | |a Calcium |
650 | 0 | 4 | |a Calcium Imaging |
650 | 0 | 4 | |a Calcium Influx |
650 | 0 | 4 | |a carboxy terminal sequence |
650 | 0 | 4 | |a Cell death |
650 | 0 | 4 | |a cell viability |
650 | 0 | 4 | |a channel gating |
650 | 0 | 4 | |a Channel Gating |
650 | 0 | 4 | |a controlled study |
650 | 0 | 4 | |a C-terminal sequences |
650 | 0 | 4 | |a Current-voltage relationship |
650 | 0 | 4 | |a electrophysiology |
650 | 0 | 4 | |a genetic transfection |
650 | 0 | 4 | |a HEK293 Cells |
650 | 0 | 4 | |a human |
650 | 0 | 4 | |a human cell |
650 | 0 | 4 | |a Humans |
650 | 0 | 4 | |a Ion Channel Gating |
650 | 0 | 4 | |a Ion Channels |
650 | 0 | 4 | |a membrane permeability |
650 | 0 | 4 | |a Mice |
650 | 0 | 4 | |a Models, Molecular |
650 | 0 | 4 | |a Mutation, Missense |
650 | 0 | 4 | |a Non-selective cation channels |
650 | 0 | 4 | |a nucleotide sequence |
650 | 0 | 4 | |a Open conformation |
650 | 0 | 4 | |a Patch Clamp |
650 | 0 | 4 | |a Peptide Mapping |
650 | 0 | 4 | |a Phosphoinositides |
650 | 0 | 4 | |a priority journal |
650 | 0 | 4 | |a promoter region |
650 | 0 | 4 | |a protein domain |
650 | 0 | 4 | |a protein protein interaction |
650 | 0 | 4 | |a Protein Structure, Secondary |
650 | 0 | 4 | |a Protein Structure, Tertiary |
650 | 0 | 4 | |a Proteins |
650 | 0 | 4 | |a Rats |
650 | 0 | 4 | |a sequence alignment |
650 | 0 | 4 | |a sequence homology |
650 | 0 | 4 | |a Signal Transduction |
650 | 0 | 4 | |a Signaling cascades |
650 | 0 | 4 | |a site directed mutagenesis |
650 | 0 | 4 | |a transient receptor potential channel 4 |
650 | 0 | 4 | |a transient receptor potential channel 5 |
650 | 0 | 4 | |a Trans-membrane domains |
650 | 0 | 4 | |a TRP Channels |
650 | 0 | 4 | |a TRPC Cation Channels |
650 | 0 | 4 | |a voltage gated potassium channel |
700 | 1 | 0 | |a Abdulmughni, A. |e author |
700 | 1 | 0 | |a Beck, A. |e author |
700 | 1 | 0 | |a Cavalié, A. |e author |
700 | 1 | 0 | |a Dettmer, V. |e author |
700 | 1 | 0 | |a Flockerzi, V. |e author |
700 | 1 | 0 | |a Helms, V. |e author |
700 | 1 | 0 | |a Jusoh, S.A. |e author |
700 | 1 | 0 | |a Philipp, S.E. |e author |
700 | 1 | 0 | |a Sell, T. |e author |
700 | 1 | 0 | |a Speicher, T. |e author |
700 | 1 | 0 | |a Stoerger, C. |e author |
700 | 1 | 0 | |a Wissenbach, U. |e author |
700 | 1 | 0 | |a Zhu, M.X. |e author |
773 | |t Journal of Biological Chemistry |