Conserved gating elements in TRPC4 and TRPC5 channels

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...

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Bibliographic Details
Main Authors: Abdulmughni, A. (Author), Beck, A. (Author), Cavalié, A. (Author), Dettmer, V. (Author), Flockerzi, V. (Author), Helms, V. (Author), Jusoh, S.A (Author), Philipp, S.E (Author), Sell, T. (Author), Speicher, T. (Author), Stoerger, C. (Author), Wissenbach, U. (Author), Zhu, M.X (Author)
Format: Article
Language:English
Subjects:
Activation analysis
Amino acid sequence
Amino Acid Substitution
Amino acids
Animals
article
biotinylation
Calcium
Calcium Imaging
Calcium Influx
carboxy terminal sequence
Cell death
cell viability
channel gating
Channel Gating
controlled study
C-terminal sequences
Current-voltage relationship
electrophysiology
genetic transfection
HEK293 Cells
human
human cell
Humans
Ion Channel Gating
Ion Channels
membrane permeability
Mice
Models, Molecular
Mutation, Missense
Non-selective cation channels
nucleotide sequence
Open conformation
Patch Clamp
Peptide Mapping
Phosphoinositides
priority journal
promoter region
protein domain
protein protein interaction
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Rats
sequence alignment
sequence homology
Signal Transduction
Signaling cascades
site directed mutagenesis
transient receptor potential channel 4
transient receptor potential channel 5
Trans-membrane domains
TRP Channels
TRPC Cation Channels
voltage gated potassium channel
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