ABCMdb

ABCC8 p.Asp854Asn

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Publications

PMID: 9521779 [PubMed] Urbatsch IL et al: "Mutations in either nucleotide-binding site of P-glycoprotein (Mdr3) prevent vanadate trapping of nucleotide at both sites."

No. Sentence Comment

265 Point mutations in the Walker A and B motifs of NB1, K719R, K719M, and D854N impaired 8-azido[R-32 P]ATP binding, whereas NB2 mutations, K1385R, K1385M, and D1506N, retained their ability to bind low concentrations of 8-azido[R-32P]ATP in the presence or absence of Mg2+ (65). Login to comment

PMID: 10674713 [PubMed] Fujita A et al: "Molecular aspects of ATP-sensitive K+ channels in the cardiovascular system and K+ channel openers."

No. Sentence Comment

567 The high-affinity binding site was saturated with 10 ␮M ATPi in the absence of Mg2ϩ i. Substitution of the conserved lysine residue in the Walker A motif (K719R and K719M) or the aspartate residue in the Walker B motif (D854N) in the first NBF all abolished the high-affinity ATPi-binding, while the corresponding mutations in the second NBF did not cause any significant effect. Login to comment
568 Because Ueda et al. (1997) and Gribble et al. (1997b) used different mutations (K719R, K719M, or D854N vs. K719A, respectively), it is not clear whether the ATPi binding found by Ueda et al. (1997) underlies the sensitization of Kir6.2 to ATPi by SUR1. Login to comment
571 The high-affinity binding site was saturated with 10 mM ATPi in the absence of Mg21 i. Substitution of the conserved lysine residue in the Walker A motif (K719R and K719M) or the aspartate residue in the Walker B motif (D854N) in the first NBF all abolished the high-affinity ATPi-binding, while the corresponding mutations in the second NBF did not cause any significant effect. Login to comment
572 Because Ueda et al. (1997) and Gribble et al. (1997b) used different mutations (K719R, K719M, or D854N vs. K719A, respectively), it is not clear whether the ATPi binding found by Ueda et al. (1997) underlies the sensitization of Kir6.2 to ATPi by SUR1. Login to comment

PMID: 15910875 [PubMed] Matsuo M et al: "KATP channel interaction with adenine nucleotides."

No. Sentence Comment

74 Mutations of either theWalkerA orWalker B motifs of NBF1, K719M and D854N abolished the high-affinity 8-azido-ATP labeling of SUR1, whereas the equivalent mutations in NBF2 did not affect it [47]. Login to comment

PMID: 10099692 [PubMed] Seino S et al: "ATP-sensitive potassium channels: a model of heteromultimeric potassium channel/receptor assemblies."

No. Sentence Comment

230 Both mutations of the lysine in the Walker A motif (K719R, K719M) and a mutation of the aspartic acid in the Walker B motif (D854N) of SUR1 impair Mg2+ -independent high-affinity ATP binding (124). Login to comment

PMID: 10601323 [PubMed] Matsuo M et al: "ATP binding properties of the nucleotide-binding folds of SUR1."

No. Sentence Comment

12 We have reported previously that mutations of either the Walker A or B motifs of NBF1, K719M, and D854N abolish the high-affinity 8-azido-ATP binding of SUR1, whereas the equivalent mutations in NBF2 do not affect ATP binding (15). Login to comment

PMID: 21540180 [PubMed] Chang N et al: "Syntaxin-1A interacts with distinct domains within nucleotide-binding folds of sulfonylurea receptor 1 to inhibit beta-cell ATP-sensitive potassium channels."

No. Sentence Comment

53 Mutants on WA and WB motifs in these truncated NBF1 (K719M and D854N, respectively) and NBF2 (K1385M and D1506N, respectively) regions were also generated (see Fig. 5A) using QuikChange௡ site-directed mutagenesis according to the manufacturer`s instructions (Stratagene, La Jolla, CA). Login to comment
191 The mutations were made by substitutions of lysine in WA and aspartic acid in WB with methionine and asparagine, respectively, and the consequent constructs are GST-NBF1-WA (K719M) (24), GST-NBF1-WB (D854N) (24, 25), GST-NBF2-WA (K1385M) (26), and GST-NBF2-WB (D1506N) (27). Login to comment
200 WB motif mutations in NBF1-WB (D854N) and NBF2-WB (D1506N) remained able to bind Syn-1A (Fig. 5B). Login to comment
201 Both NBF1-WB (D854N) and NBF2-WB (D1506N) were also as effective as their wild type proteins in blocking Syn-1A inhibition of INS-1 beta-cell KATP channels (Fig. 5D and representative traces in supplemental Fig. S2) and in disrupting Syn-1A interactions with full-length SUR1 in the FRET assay (supplemental Fig. S3). Login to comment
247 Conserved aspartic acid residues were substituted with asparagines, generating NBF1-WB (D854N) and NBF2-WB (D1506N) truncated proteins. Login to comment
249 Panel (i), NBF-1: WA motif mutant NBF1-WA (K719M) could not bind Syn-1A, whereas WB motif mutant NBF1-WB (D854N) remained able to bind Syn-1A. Full-length NBF1, WT NBF1-WA, and WT NBF1-WB are positive controls. Login to comment
257 FRET studies shown in supplemental Fig. S3 demonstrated that WB motif mutants including NBF1-WB (D854N) and NBF2-WB (D1506N), like their corresponding wild type proteins, disrupted Syn-1A interactions with SUR1. Login to comment
259 WB motif mutants NBF1-WB (D854N) and NBF2-WB (D1506N), like their WT proteins, remained able to block Syn-1A inhibition of KATP channels. Login to comment
189 The mutations were made by substitutions of lysine in WA and aspartic acid in WB with methionine and asparagine, respectively, and the consequent constructs are GST-NBF1-WA (K719M) (24), GST-NBF1-WB (D854N) (24, 25), GST-NBF2-WA (K1385M) (26), and GST-NBF2-WB (D1506N) (27). Login to comment
198 WB motif mutations in NBF1-WB (D854N) and NBF2-WB (D1506N) remained able to bind Syn-1A (Fig. 5B). Login to comment
199 Both NBF1-WB (D854N) and NBF2-WB (D1506N) were also as effective as their wild type proteins in blocking Syn-1A inhibition of INS-1 beta-cell KATP channels (Fig. 5D and representative traces in supplemental Fig. S2) and in disrupting Syn-1A interactions with full-length SUR1 in the FRET assay (supplemental Fig. S3). Login to comment
250 Conserved aspartic acid residues were substituted with asparagines, generating NBF1-WB (D854N) and NBF2-WB (D1506N) truncated proteins. Login to comment
252 Panel (i), NBF-1: WA motif mutant NBF1-WA (K719M) could not bind Syn-1A, whereas WB motif mutant NBF1-WB (D854N) remained able to bind Syn-1A. Full-length NBF1, WT NBF1-WA, and WT NBF1-WB are positive controls. Login to comment
261 FRET studies shown in supplemental Fig. S3 demonstrated that WB motif mutants including NBF1-WB (D854N) and NBF2-WB (D1506N), like their corresponding wild type proteins, disrupted Syn-1A interactions with SUR1. Login to comment
263 WB motif mutants NBF1-WB (D854N) and NBF2-WB (D1506N), like their WT proteins, remained able to block Syn-1A inhibition of KATP channels. Login to comment

PMID: 10570926 [PubMed] Matsuo M et al: "NEM modification prevents high-affinity ATP binding to the first nucleotide binding fold of the sulphonylurea receptor, SUR1."

No. Sentence Comment

64 We have reported previously that mutations in either the Walker A or B motifs of NBF1, K719M and D854N, abolish Fig. 1. Login to comment

PMID: 10194514 [PubMed] Miki T et al: "The structure and function of the ATP-sensitive K+ channel in insulin-secreting pancreatic beta-cells."

No. Sentence Comment

97 Mutations of Walker A (K719R and K719M) in NBF-1 and Walker B (D854N) in NBF-1 of SUR1 severely impair Mg2+ -independent high-affinity ATP binding. Login to comment

PMID: 9287292 [PubMed] Ueda K et al: "MgADP antagonism to Mg2+-independent ATP binding of the sulfonylurea receptor SUR1."

No. Sentence Comment

61 Substitutions of the conserved lysine in Walker A, K719R and K719M (lanes 2 and 3), or the aspartate in Walker B, D854N (lane 4), abolished the binding of 5 ␮M 8-azido-[␣-32 P]ATP, although substitutions at equivalent sites in NBF2, K1385R, K1385M, or D1506N (lanes 5, 6, and 7) did not affect it. SUR1 with mutations in NBF1 binds ATP only slightly even when incubated with 40 ␮M 8-azido-[␣-32 P]ATP. Login to comment
103 Lane 1, wild-type SUR1; lane 2, K719R; lane 3, K719M; lane 4, D854N; lane 5, K1385R; lane 6, K1385M; lane 7, D1506N. Login to comment