ABCMdb

ABCC7 p.Thr1115Cys

None has been submitted yet.

Publications

PMID: 23955087 [PubMed] Wang W et al: "Relative contribution of different transmembrane segments to the CFTR chloride channel pore."

No. Sentence Comment

4 Two accessible residues in TM11 (T1115C and S1118C) were found to be more readily modified from the extracellular solution in closed channels, but more readily modified from the intracellular solution in open channels, as previously reported for T338C in TM6. Login to comment
77 Note that while MTSES caused rapid inhibition of macroscopic current amplitude in T1115C and S1118C, inhibition of I1112C current was much slower (note different time scale for this mutant). Login to comment
111 b Example whole cell currents recorded continuously at +30 mV for constitutively active T1115C/ E1371Q and S1118C/E1371Q channels. Login to comment
112 In contrast to currents carried by T1115C and S1118C channels (see Fig. 3), these whole cell currents were not significantly affected by addition of 200 bc;M MTSES to the extracellular solution (black bars), even though these currents were positively identified as being carried by CFTR by sensitivity to GlyH-101 (50 bc;M, hatched bars). Login to comment
117 Application of MTSES (200 bc;M) following channel activation with PKA and ATP caused a decrease in macroscopic current amplitude in I1112C, T1115C and S1118C, but not in T1121C (Fig. 2a, b) or in I1109C, F1110C, F1111C, A1113C, V1114C, F1116C, or I1117C (Fig. 2c). Login to comment
123 Figure 3 confirms that application of external MTSES (200 bc;M) following channel activation with cAMP-stimulatory cocktail caused a decrease in whole cell current amplitude in T1115C, S1118C, and T1121C, but not in I1112C. Login to comment
127 State-dependent accessibility of T1115C and S1118C in TM11 Modification of T1115C and S1118C by both internal and external MTSES is reminiscent of the accessibility pattern observed for TM6 cysteine mutant T338C [42]. Login to comment
137 As shown in Fig. 4a, c, the E1371Q mutation significantly accelerated the rate of modification of both T1115C and S1118C by intracellular MTSES, suggesting that these cysteines are more readily modified from the inside in open channels. Login to comment
199 Furthermore, using the same approach used previously to study side-dependent modification of T338C [42], we found that T1115C and S1118C were more readily modified from the extracellular solution in closed channels, but more readily modified from the intracellular solution in open channels (Fig. 4). Login to comment