ABCMdb

ABCC7 p.Val232Lys

None has been submitted yet.

Publications

PMID: 19181854 [PubMed] Rath A et al: "Detergent binding explains anomalous SDS-PAGE migration of membrane proteins."

No. Sentence Comment

42 We noted that certain hairpins ran as more diffuse bands than others (e.g., P205S and Q220W vs. V232K and E217V, see Fig. 1B). Login to comment
62 V232D, V232A, P205S, and Q220W) migrated as WT within statistical significance; 2 were faster (V232D and V232K); and 4 were slower (G228L, E217V, E217F, and E217S/S222E). Login to comment
85 Gel shifts, SDS binding, helicity, and column MW of TM3/4 hairpins Hairpin* Gel shift (dMW, %) Bound SDS (g/g) Helicity (MRE X 103)† Column MW (mut-wt, %)‡ V232Dcf -11 Ϯ 2.6 3.4 Ϯ 0.9 -17 Ϯ 1.2 ϩ19 Ϯ 1.5 V232K -10 Ϯ 3.0 3.8 Ϯ 0.6 -16 Ϯ 1.1 ϩ5.6 Ϯ 1.6 A204L -2.2 Ϯ 2.3 6.0 Ϯ 0.7 -18 Ϯ 1.3 ϩ3.4 Ϯ 1.6 P205A/V232Dcf ϩ0.12 Ϯ 5.2 4.7 Ϯ 0.4 -19 Ϯ 2.6 ϩ21 Ϯ 0.6 WT ϩ0.42 Ϯ 4.5 5.4 Ϯ 1.4 -18 Ϯ 2.2 0.0 Ϯ 0.79 V232A ϩ3.6 Ϯ 3.7 5.2 Ϯ 0.4 -18 Ϯ 0.9 ϩ6.1 Ϯ 1.9 P205Scf ϩ4.7 Ϯ 6.0 4.7 Ϯ 1.0 -18 Ϯ 0.7 ϩ4.4 Ϯ 1.6 Q220W ϩ6.3 Ϯ 2.4 5.0 Ϯ 0.7 -21 Ϯ 2.7 -4.9 Ϯ 1.3 G228L ϩ14 Ϯ 5.1 6.9 Ϯ 1.4 -23 Ϯ 1.7 ϩ14 Ϯ 2.6 E217V ϩ28 Ϯ 1.3 6.7 Ϯ 1.0 -25 Ϯ 1.7 ϩ32 Ϯ 4.0 E217F ϩ29 Ϯ 2.8 9.4 Ϯ 1.9 -28 Ϯ 2.6 ϩ17 Ϯ 1.1 E217S/S222E ϩ29 Ϯ 7.6 10 Ϯ 2.3 -25 Ϯ 2.8 ϩ35 Ϯ 0.9 Glycophorin§ - 3.4 Ϯ 0.6 -9.5 Ϯ 1.2 ϩ83 Ϯ 5.1 *Mutant hairpins are listed in order of increasing gel shift. Login to comment

PMID: 24412276 [PubMed] Loo TW et al: "The cystic fibrosis V232D mutation inhibits CFTR maturation by disrupting a hydrophobic pocket rather than formation of aberrant interhelical hydrogen bonds."

No. Sentence Comment

134 To test if other charged amino acids inhibited maturation, we constructed mutants V232R and V232K. Login to comment
160 We tested if mutations to Val232 that severely inhibited maturation (V232E, V232K, or V232R) could be rescued with other correctors predicted to act as pharmacological chaperones such as 4a [33], VX-809 [19], 2b [35], 5a [12], or VX-325 [36]. Login to comment
164 Mutant V232K was rescued with correctors 4a, VX-809 and VX-325 (25-60% mature product) (Fig. 4B and D) while mutant V232R could only be rescued with VX-809 (about 25% mature product) (Fig. 4C and D). Login to comment
171 Accordingly, we introduced the V510D suppressor mutation into mutants V232E, V232K, or V232R. Login to comment
175 The V510D suppressor caused a small increase in the amount of V232K mature protein (10%) but no detectable increase was observed in mutant V232R when expressed in the absence of VX-809 (Fig. 5A and B). Login to comment
176 The V510D/V232K mutant however, could still be efficiently rescued with corrector VX-809 to yield mature CFTR as the major product (about 70%). Login to comment
177 The relative maturation levels achieved using correctors or the V510D suppressor show that the V232E mutation could be more efficiently rescued than the V232K or V232R mutations. Login to comment
188 Fig. 4. Rescue of V232E, V232K, and V232R mutants with correctors. Login to comment
189 Whole cell extracts of cells expressing mutants V232E (A), V232K (B), or V232R (C) in the absence (none) or presence of various correctors were subjected to immunoblot analysis. Login to comment
195 The L305R(TM5) P-gp mutant resembles CFTR mutants V232D, V232E, and V232K The characteristics of the V232D/Q207X (Fig. 1) and V232X (Fig. 3) mutants suggest that the mechanism of the V232D mutation involves disruption of a hydrophobic pocket between TM segments. Login to comment
204 It appears that the CFTR V232D, V232E, and V232K processing mutationsresemble P-gp mutantsthatcontain acharged residueata hydrophobic interface between adjacent TM segments because they can be efficiently rescued (with VX-809). Login to comment
222 (A) Whole cell extracts of cells expressing CFTR mutants V232E/V510D, V232K/V510D or V232R/ V510D in the absence () or presence (+) of VX-809 or were subjected to immunoblot analysis. Login to comment