ABCMdb

ABCC8 p.Lys719Arg

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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: 10204114 [PubMed] Aguilar-Bryan L et al: "Molecular biology of adenosine triphosphate-sensitive potassium channels."

No. Sentence Comment

526 For example, the K719R mutation in the conserved Walker A motif that is involved in binding of the ␣- and beta-phosphates has no effect on the ATP sensitivity of reconstituted channels (190), although Ueda et al. (239) show that SUR1K719R does not photolabel with [32 P] 8-azido ATP. Login to comment

PMID: 9755153 [PubMed] Schwanstecher M et al: "Potassium channel openers require ATP to bind to and act through sulfonylurea receptors."

No. Sentence Comment

114 However, by analogy with the results seen with SUR2B, substitution of a lysine for an arginine in either NBF of SUR1 (K719R and/or K1384R) eliminates diazoxide binding and induces a complete loss of activation of SUR1/KIR6.2 channels (results not shown). Login to comment

PMID: 18281290 [PubMed] Babenko AP et al: "A novel ABCC8 (SUR1)-dependent mechanism of metabolism-excitation uncoupling."

No. Sentence Comment

80 Second, K719R plus K1384R in the Walker A motifs eliminated the differences between the two channel activities on-cell and in 1 mM MgATP; the fractions of the Pomax were 0.003 Ϯ 0.0012 and 0.0034 Ϯ 0.0018 versus 0.0025 Ϯ 0.001 and 0.0028 Ϯ 0.0011 for NDSUR1K719RϩK1384R versus SUR1K719RϩK1384R channel, respectively (n ϭ 3 for each). Login to comment

PMID: 9202152 [PubMed] Inagaki N et al: "Subunit stoichiometry of the pancreatic beta-cell ATP-sensitive K+ channel."

No. Sentence Comment

32 The K719R mutation in the Walker A motif [4,16] in the first nucleotide-binding fold (NBF)-l of SURI and the G132S mutation in the H5 region of Kir6.2 were introduced using 21-mer oligonucleotides according to the manufacturer's instructions (in vitro mutagenesis system, Promega). Login to comment
129 Mutß, the mutant ß of which amino acid residue lysine-719 was mutated to arginine. 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: 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