Regions involved in the opening of CIC-2 chloride channel by voltage and cell volume

Article Abstract:

The chloride channel CIC-2 has a general role in cell volume regulation since it can be activated by hypotonicity in the extracellular medium. The domains responsible for activation by both volume and voltage are located on its amino terminus. The channel remains open and does not respond to the tonicity of the medium if a mutation occurs in an essential region. A deletion in a modulating region, however, produces partially open channels that respond to both increased and decreased tonicity. These domains retain their function when transplanted to different regions of the protein.

Cellular control mechanisms, Cell regulation

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Two physically distinct pores in the dimeric CIC-0 chloride channel

Article Abstract:

The chloride channel CIC-0 of the torpedo regulates electric excitability and transepithelial transport by producing impulse bursts with two identical conductance levels about 8pS. Introduction of serine 123 alters rectification, ion selectivity and gating but does not affect bursting behavior. The results indicate that the conductance, ion selectivity and gating of CIC-0 is determined only by a single subunit forming a single pore. The results also suggest that CIC-0 is a homodimer with two largely independent pores.

Fishes, Ion channels, Neural transmission, Synaptic transmission

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Gating of the voltage-dependent chloride channel ClC-0 by the permeant anion

Article Abstract:

A study of the torpedo channel ClC-0, a type of chloride channel, indicates that the external chloride ions induce gating or opening of the channel. This gating phenomenon depends on voltage and occurs most efficiently only when Cl- is the gating charge. Gating kinetics, ion preference and dependence on concentration vary with the removal of a positive charge present in the D12 domain's cytoplasmic end.

Anions

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