In the beginning: a personal reminiscence on the origin and legacy of ClC-0, the 'Torpedo Cl(-) channel'.
نویسنده
چکیده
This unapologetically subjective essay recalls the Torpedo Cl(-) channel in the years when it had neither a molecular identity nor proper name (ClC-0), and membership in a large superfamily. I discuss the circumstances surrounding its discovery and subsequent research through the 1980s that revealed its unusual molecular architecture and other strange mechanistic characteristics.
منابع مشابه
Nonequilibrium gating and voltage dependence of the ClC-0 Cl- channel
The gating of ClC-0, the voltage-dependent Cl- channel from Torpedo electric organ, is strongly influenced by Cl- ions in the external solution. Raising external Cl- over the range 1-600 mM favors the fast-gating open state and disfavors the slow-gating inactivated state. Analysis of purified single ClC-0 channels reconstituted into planar lipid bilayers was used to identify the role of Cl- ion...
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Single-channel recordings of the currents mediated by the muscle Cl- channel, ClC-1, expressed in Xenopus oocytes, provide the first direct evidence that this channel has two equidistant open conductance levels like the Torpedo ClC-0 prototype. As for the case of ClC-0, the probabilities and dwell times of the closed and conducting states are consistent with the presence of two independently ga...
متن کاملIntracellular Proton Regulation of ClC-0
Some CLC proteins function as passive Cl(-) ion channels whereas others are secondary active chloride/proton antiporters. Voltage-dependent gating of the model Torpedo channel ClC-0 is modulated by intracellular and extracellular pH, possibly reflecting a mechanistic relationship with the chloride/proton coupling of CLC antiporters. We used inside-out patch clamp measurements and mutagenesis to...
متن کاملInward Rectification in ClC-0 Chloride Channels Caused by Mutations in Several Protein Regions
Several cloned ClC-type Cl- channels open and close in a voltage-dependent manner. The Torpedo electric organ Cl- channel, ClC-0, is the best studied member of this gene family. ClC-0 is gated by a fast and a slow gating mechanism of opposite voltage direction. Fast gating is dependent on voltage and on the external and internal Cl- concentration, and it has been proposed that the permeant anio...
متن کاملSide-chain Charge Effects and Conductance Determinants in the Pore of ClC-0 Chloride Channels
The charge on the side chain of the internal pore residue lysine 519 (K519) of the Torpedo ClC-0 chloride (Cl-) channel affects channel conductance. Experiments that replace wild-type (WT) lysine with neutral or negatively charged residues or that modify the K519C mutant with various methane thiosulfonate (MTS) reagents show that the conductance of the channel decreases when the charge at posit...
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عنوان ژورنال:
- The Journal of physiology
دوره 593 18 شماره
صفحات -
تاریخ انتشار 2015