Figure 1.
Figure 1. Cysless CFTR is an appropriate background for cysteine scanning. (A) Topological diagram of CFTR showing its domain architecture: two TMDs, two NBDs, and one R domain. Each TMD contains six TMs (1–6 and 7–12) connected by intracellular and extracellular loops. Cysteines were introduced into TM6 (yellow). The sequence of TM6 is shown, and residues where cysteine-substitution affects single-channel amplitude are indicated by stars. (B and C) Modification of phosphorylated WT CFTR channels by MTSET and MTSES. After the ATP-induced current reached a plateau, the solution was exchanged from ATP to ATP plus MTSES or MTSET using the fast solution exchange system (see Materials and methods). The solution was switched back to ATP after the MTS reagents took full effect. The dotted line represents the baseline in all figures. (D and E) Similar protocols as in B and C showing that cysless CFTR channels do not respond to the treatment of MTS.

Cysless CFTR is an appropriate background for cysteine scanning. (A) Topological diagram of CFTR showing its domain architecture: two TMDs, two NBDs, and one R domain. Each TMD contains six TMs (1–6 and 7–12) connected by intracellular and extracellular loops. Cysteines were introduced into TM6 (yellow). The sequence of TM6 is shown, and residues where cysteine-substitution affects single-channel amplitude are indicated by stars. (B and C) Modification of phosphorylated WT CFTR channels by MTSET and MTSES. After the ATP-induced current reached a plateau, the solution was exchanged from ATP to ATP plus MTSES or MTSET using the fast solution exchange system (see Materials and methods). The solution was switched back to ATP after the MTS reagents took full effect. The dotted line represents the baseline in all figures. (D and E) Similar protocols as in B and C showing that cysless CFTR channels do not respond to the treatment of MTS.

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