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The Journal of Neuroscience, February 15, 2003, 23(4):1340
Functional Role of C-Terminal Cytoplasmic Tail of Rat Vanilloid
Receptor 1
Viktorie
Vlachová1,
Jan
Teisinger1,
Klára
Su ánková1,
Alla
Lyfenko1,
Rüdiger
Ettrich2, 3, and
Ladislav
Vyklický1
1 Institute of Physiology, Academy of Sciences, 142 20 Prague 4, Czech Republic, 2 Institute of Physical Biology,
University of South Bohemia, 373 33 Nové Hrady, Czech Republic,
and 3 Department of Biochemistry, Faculty of Science,
Charles University, 128 40 Prague 2, Czech Republic
The vanilloid receptor [transient receptor potential (TRP)V1, also
known as VR1] is a member of the TRP channel family. These receptors
share a significant sequence homology, a similar predicted structure
with six transmembrane-spanning domains (S1-S6), a pore-forming region
between S5 and S6, and the cytoplasmically oriented C- and N-terminal
regions. Although structural/functional studies have identified some of
the key amino acids influencing the gating of the TRPV1 ion channel,
the possible contributions of terminal regions to vanilloid receptor
function remain elusive. In the present study, C-terminal truncations
of rat TRPV1 have been constructed to characterize the contribution of
the cytoplasmic C-terminal region to TRPV1 function and to delineate
the minimum amount of C tail necessary to form a functional channel.
The truncation of 31 residues was sufficient to induce changes in
functional properties of TRPV1 channel. More pronounced effects of
C-terminal truncation were seen in mutants lacking the final 72 aa.
These changes were characterized by a decline of capsaicin-,
pH-, and heat-sensitivity; progressive reduction of the
activation thermal threshold (from 41.5 to 28.6°C); and slowing of
the activation rate of heat-evoked membrane currents
(Q10 from 25.6 to 4.7). The
voltage-induced currents of the truncated mutants exhibited a slower
onset, markedly reduced outward rectification, and significantly smaller peak tail current amplitudes. Truncation of the entire TRPV1
C-terminal domain (155 residues) resulted in a nonfunctional channel.
These results indicate that the cytoplasmic COOH-terminal domain
strongly influences the TRPV1 channel activity, and that the distal
half of this structural domain confers specific thermal sensitivity.
Key words:
capsaicin receptor; TRPV1; C-terminal domain; heat
transduction; heat sensitivity; voltage-gated cation channel
Copyright © 2003 Society for Neuroscience 0270-6474/03/2341340-11$05.00/0
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