Transmembrane topology of a CLC chloride channel
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Key result
Using in vitro glycosylation scanning and protease protection assays, the ClC-1 chloride channel was shown to have 10 or 12 transmembrane domains with both N and C termini facing the cytoplasm.
Population
human ClC-1 chloride channel studied via in vitro translation and Xenopus oocytes
Design
Preclinical
Authors
Discussion
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Implication
Aids interpretation of myotonia-linked ClC-1 mutations; leaves open in vivo validation before clinical translation.
Structured PICO
P
Population
human ClC-1 chloride channel (prototype CLC channel defective in human myotonia) studied via in vitro translation and Xenopus oocytes
I
Intervention
In vitro glycosylation scanning, protease protection assays, and cysteine scanning
O
Outcome
Transmembrane topology of human ClC-1
This study maps the transmembrane topology of the human ClC-1 chloride channel, providing a structural basis for understanding mutations that cause human myotonia.
Limitations
- Most hydrophilic loops of ClC-1 are shorter than 33 residues, which is a lower limit for reliable glycosylation.
- Enzymatic modification of residues may be hindered by steric constraints.
Cite This Study
Schmidt‐Rose et al. (1997) studied ClC-1 chloride channel topology. Using in vitro glycosylation scanning and protease protection assays, the ClC-1 chloride channel was shown to have 10 or 12 transmembrane domains with both N and C termini facing the cytoplasm.
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