ABCMdb

ABCC8 p.Lys719Met

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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
83 We found that the K719M mutation of SUR1 affects 8-azido-ATP binding not only to NBF1 but also to NBF2 (Matsuo M, et al., unpublished data). Login to comment

PMID: 19151370 [PubMed] Pratt EB et al: "Sulfonylurea receptor 1 mutations that cause opposite insulin secretion defects with chemical chaperone exposure."

No. Sentence Comment

124 We therefore tested the effect of R74W or E128K on channel ATP sensitivity in the background of SUR1-NBD mutations such as G1479D and G1479R in NBD2 and K719M in NBD1, which are known to abolish channel response to MgADP stimulation (28). Login to comment
126 We also combined E128K with NBD1 mutation K719M (E128K/K719M), and the resulting channels were as insensitive to ATP as E128K (not shown). Login to comment

PMID: 15218066 [PubMed] Prost AL et al: "Zinc is both an intracellular and extracellular regulator of KATP channel function."

No. Sentence Comment

162 KATP channels with impaired nucleotide binding domains are still activated by intracellular Zn2+ Channel activity was measured at -30 mV in inside-out patches excised from Xenopus oocytes coinjected with Kir6.2 and SUR1(K719M,K1385M) or SUR2A(D832N,D1469N). Login to comment
163 A, activation by 20 µM Zn2+ of SUR1(K719M,K1385M)/Kir6.2 channels. B, average currents in 100 µM ATP measured before or during application of 20 µM Zn2+. 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

8 Only NBF1-WA (K719M) or NBF2-WA (K1385M) mutant no longer bound to Syn-1A; K1385M failed to disrupt Syn-1A-mediated inhibition of KATP channels. Login to 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
193 The WA motif mutations in NBF1-WA (K719M) (Fig. 5B, panel (i)) and NBF2-WA (K1385M) (Fig. 5B, panel (ii)) did not bind Syn-1A in contrast to its respective wild type proteins (Fig. 1B). Login to comment
194 Because NBF1-WA (wt) domain did not disrupt Syn-1A/ SUR1 interactions on our FRET or patch clamp studies (Figs. 2-4 and supplemental Fig. S1), we did not further examine NBF1-WA (K719M). Login to comment
246 Conserved lysine residues in WA motifs were substituted with methionine, generating NBF1-WA (K719M) and NBF2-WA (K1385M) 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
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
192 Because NBF1-WA (wt) domain did not disrupt Syn-1A/ SUR1 interactions on our FRET or patch clamp studies (Figs. 2-4 and supplemental Fig. S1), we did not further examine NBF1-WA (K719M). 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

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

25 Hamster SUR1 (K719M) cDNA was generously provided by Dr Susumu Seino (Chiba University, Japan). Login to comment
63 However, the K719M mutant form of SUR1 (in which the lysine residue within the Walker A motif of NBF1 was replaced with methionine) was not photoa¤nity labeled either in the absence or in the presence of NEM. These results indicate that cysteine-717 within NBF1 of SUR1 is responsible for inhibition of high-a¤nity 8-azido-ATP binding by NEM, and suggest that NBF1 of SUR1 has a NEM-sensitive structure similar to that of NBF1 of MDR1. Login to 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
85 Acknowledgements: We thank Dr S. Seino (Chiba University, Japan) for providing hamster SUR1 (K719M) cDNA and the antibody against SUR1. Login to comment

PMID: 17317760 [PubMed] Masia R et al: "A mutation in the TMD0-L0 region of sulfonylurea receptor-1 (L225P) causes permanent neonatal diabetes mellitus (PNDM)."

No. Sentence Comment

117 Consistent with this, the effects of L225P on channel activity in the intact cell were abolished by combination with either of two NBF mutations (K719M or D1506A) that abolish Mg-nucleotide stimulation of the channel (19,20) (Fig. 2D). Login to comment
118 Consistent with this, the effects of L225P on channel activity in the intact cell were abolished by combination with either of two NBF mutations (K719M or D1506A) that abolish Mg-nucleotide stimulation of the channel (19,20) (Fig. 2D). 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
96 However, we have observed that while K719M and K719R mutants severely impair functional expression of KATP channels, K1385M and K1385R mutants do not.2 Although whether or not SUR1 has ATP hydrolysis activity is unknown, ATP binding to NBF1 of SUR1 might be important in maintaining KATP channels in the operative state. 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