scholarly journals Molecular and functional characterization of the voltage-gated proton channel in zebrafish neutrophils

2017 ◽  
Vol 5 (15) ◽  
pp. e13345 ◽  
Author(s):  
Adisorn Ratanayotha ◽  
Takafumi Kawai ◽  
Shin-ichi Higashijima ◽  
Yasushi Okamura
2003 ◽  
Vol 53 (1-2) ◽  
pp. 107-117 ◽  
Author(s):  
Patrick Cossette ◽  
Andrew Loukas ◽  
Ronald G. Lafrenière ◽  
Daniel Rochefort ◽  
Eric Harvey-Girard ◽  
...  

FEBS Letters ◽  
1991 ◽  
Vol 295 (1-3) ◽  
pp. 211-213 ◽  
Author(s):  
T.Ann Blair ◽  
Steven L. Roberds ◽  
Michael M. Tamkun ◽  
Robert P. Hartshorne

2009 ◽  
Vol 7 (1) ◽  
pp. 71 ◽  
Author(s):  
Francisco M Pinto ◽  
Cristina G Ravina ◽  
Manuel Fernández-Sánchez ◽  
Manuel Gallardo-Castro ◽  
Antonio Cejudo-Román ◽  
...  

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Qingfeng Chen ◽  
Weizhong Zeng ◽  
Ji She ◽  
Xiao-chen Bai ◽  
Youxing Jiang

The otopetrin (OTOP) proteins were recently characterized as proton channels. Here we present the cryo-EM structure of OTOP3 from Xenopus tropicalis (XtOTOP3) along with functional characterization of the channel. XtOTOP3 forms a homodimer with each subunit containing 12 transmembrane helices that can be divided into two structurally homologous halves; each half assembles as an α-helical barrel that could potentially serve as a proton conduction pore. Both pores open from the extracellular half before becoming occluded at a central constriction point consisting of three highly conserved residues – Gln232/585-Asp262/Asn623-Tyr322/666 (the constriction triads). Mutagenesis shows that the constriction triad from the second pore is less amenable to perturbation than that of the first pore, suggesting an unequal contribution between the two pores to proton transport. We also identified several key residues at the interface between the two pores that are functionally important, particularly Asp509, which confers intracellular pH-dependent desensitization to OTOP channels.


1988 ◽  
Vol 136 (1) ◽  
pp. 383-403 ◽  
Author(s):  
C. A. Loretz ◽  
C. R. Fourtner

An anion channel was isolated, using patch-clamp technique, from the basolateral membrane of goby intestinal epithelial cells. Single-channel conductance varied over a range from 20 to 90 pS. The channel was voltage-gated over the physiological range of cell membrane potential with depolarization increasing the proportion of time in the open state. There was no Ca2+ sensitivity. The selectivity sequence was SO4(2-) greater than Cl- greater than Mes-. The channel may function in vivo as one of several avenues of basolateral membrane Cl- exit with the voltage-gating property serving to match basolateral Cl- exit to apical entry.


2019 ◽  
Author(s):  
Qingfeng Chen ◽  
Weizhong Zeng ◽  
Ji She ◽  
Xiao-chen Bai ◽  
Youxing Jiang

PLoS ONE ◽  
2010 ◽  
Vol 5 (11) ◽  
pp. e14081 ◽  
Author(s):  
Gábor L. Petheő ◽  
Anna Orient ◽  
Mónika Baráth ◽  
István Kovács ◽  
Bence Réthi ◽  
...  

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