ABCMdb

ABCB7 p.Glu433Lys

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Publications

PMID: 22884976 [PubMed] Liesa M et al: "Mitochondrial ABC transporters function: the role of ABCB10 (ABC-me) as a novel player in cellular handling of reactive oxygen species."

No. Sentence Comment

96 The heritage family study shows that the amino acid change of E433K at the C-terminal of the sixth TMD [9,70] or V411L at the beginning of the sixth TMD in ABCB7 is sufficient to cause XLSA/A [56]. Login to comment

PMID: 21464130 [PubMed] Gonzalez-Cabo P et al: "Disruption of the ATP-binding cassette B7 (ABTM-1/ABCB7) induces oxidative stress and premature cell death in Caenorhabditis elegans."

No. Sentence Comment

21 The third mutation produces a more substantial amino acid change E433K (5). Login to comment
22 A human cDNA containing the E433K change is able to partially rescue yeast carrying a mutation in ATM1, the homologue of ABCB7, suggesting that this change does not cause a complete loss of function (5). Login to comment

PMID: 20481466 [PubMed] Ye H et al: "Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease."

No. Sentence Comment

227 In the second family, a single missense mutation is found in exon 10 of the ABCB7 gene in two affected brothers, and the mutation is a G-to-A transition at nucleotide 1305, resulting in a Glu-to-Lys substitution at residue 433 (E433K) in the putative sixth transmembrane domain of ABCB7 (72). Login to comment
228 In the third family, the affected brothers have a G-to-C transition at position 1299, which predicts a V411L substitution in the sixth putative transmembrane domain (86). Login to comment

PMID: 18637800 [PubMed] Camaschella C et al: "Recent advances in the understanding of inherited sideroblastic anaemia."

No. Sentence Comment

132 The missense mutations (Ile400 Met Glu 433Lys, Val 411Leu) reported in patients are unable to rescue the Atm1p-deficient phenotype, indicating that they are partial loss of function mutations (reviewed in Fleming, 2002). Login to comment

PMID: 17192398 [PubMed] Pondarre C et al: "Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis."

No. Sentence Comment

7 Materials and methods The generation of a conditionally targeted ("floxed") allele of Abcb7 (Abcb7fl) has been described previously.10 A targeted point mutant allele was made by site-directed mutagenesis (QuickChange; Stratagene, La Jolla, CA) of the original gene targeting construct to create a glutamic acid-to- lysine mutation at position 433 (E433K) of the mouse protein corresponding to the hematologically most severe, E433K, human allele.2 All exons and intron/exon boundaries were resequenced in the mutagenized targeting construct. Login to comment
37 In order to circumvent the bone marrow-dependent lethality, we created a targeted point mutant allele corresponding to the hematologically most severe human E433K mutation.2 Male chimeras were, however, infertile due to testicular atrophy and incomplete spermatogenesis associated with interstitial iron deposition (not shown), which is a phenotype not reported in human subjects with XLSA/A. Login to comment
6 Materials and methods The generation of a conditionally targeted ("floxed") allele of Abcb7 (Abcb7fl) has been described previously.10 A targeted point mutant allele was made by site-directed mutagenesis (QuickChange; Stratagene, La Jolla, CA) of the original gene targeting construct to create a glutamic acid-to- lysine mutation at position 433 (E433K) of the mouse protein corresponding to the hematologically most severe, E433K, human allele.2 All exons and intron/exon boundaries were resequenced in the mutagenized targeting construct. Login to comment
36 In order to circumvent the bone marrow-dependent lethality, we created a targeted point mutant allele corresponding to the hematologically most severe human E433K mutation.2 Male chimeras were, however, infertile due to testicular atrophy and incomplete spermatogenesis associated with interstitial iron deposition (not shown), which is a phenotype not reported in human subjects with XLSA/A. Login to comment

PMID: 17192393 [PubMed] Cavadini P et al: "RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload."

No. Sentence Comment

15 They consist of missense mutations (I400M, E433K, and V411L) at the border of putative transmembrane domains of the protein and were found to rescue only partially the defects of Atm1p-deficient yeasts.6 A study on erythroid cells showed that ABCB7 expression increases the activity of ferrochelatase by binding to its C-terminus.21 The recent study of mice deficient in ABCB7 showed that the protein is essential in early gestation. Login to comment
13 (c) 2007 by The American Society of Hematology 3552 They consist of missense mutations (I400M, E433K, and V411L) at the border of putative transmembrane domains of the protein and were found to rescue only partially the defects of Atm1p-deficient yeasts.6 A study on erythroid cells showed that ABCB7 expression increases the activity of ferrochelatase by binding to its C-terminus.21 The recent study of mice deficient in ABCB7 showed that the protein is essential in early gestation. Login to comment

PMID: 11843825 [PubMed] Maguire A et al: "X-linked cerebellar ataxia and sideroblastic anaemia associated with a missense mutation in the ABC7 gene predicting V411L."

No. Sentence Comment

137 Furthermore, the predicted amino acid substitutions arising from previously reported mutations I400M (Allikmets et al, 1999) and E433K (Bekri et al, 2000) and that reported here at residue 411 highlight the importance of this region of the protein in iron homeostasis and ataxia. Login to comment

PMID: 11050011 [PubMed] Bekri S et al: "Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation."

No. Sentence Comment

6 The mutation was a G-to-A transition at nucleotide 1305 of the full-length cDNA, resulting in a charge inversion caused by the substitution of lysine for glutamate at residue 433 C-terminal to the putative sixth transmembrane domain of ABC7. Login to comment
9 In contrast, the expression of mutated ABC7 (E433K) or Atm1p (D398K) proteins in ⌬atm1 cells led to a low efficiency of cytosolic Fe/S protein maturation. Login to comment
164 The mutation resulted in a substitution of lysine for the wild-type glutamate at amino acid 433 (E433K) of the ABC7 protein and abolished a BsmAI restriction site (Figure 1D). Login to comment
169 In addition, we performed similar studies with Atm1p into which the mutation corresponding to the human ABC7 mutant (E433K) was introduced (Atm1p D398K). Login to comment
170 Wild-type Atm1p and, to a slightly lesser extent, ABC7 complemented the growth defect of ⌬atm1 cells and the defect leading to mitochondrial iron accumulation.12 Similarly, both the Atm1p D398K and the ABC7 E433K mutant proteins restored growth of ⌬atm1 cells to a similar extent as the corresponding wild-type proteins (data not shown). Login to comment
177 Finally, we investigated the consequences of the XLSA/A mutation E433K in ABC7 and the corresponding mutation in Atm1p (D398K) for the function of these proteins in cytosolic Fe/S protein maturation. Login to comment
206 These results represent the second mutation in the human ABC7 gene and therefore confirm and extend the previous identification of an ABC7 mutation (1208T3G) that substituted a methionine for an isoleucine at codon 400 in exon 9 as the cause of XLSA/A. Login to comment
210 The E433K mutation in ABC7 identified in this XLSA/A family impaired the function of the protein in cytosolic Fe/S protein assembly. Login to comment
5 The mutation was a G-to-A transition at nucleotide 1305 of the full-length cDNA, resulting in a charge inversion caused by the substitution of lysine for glutamate at residue 433 C-terminal to the putative sixth transmembrane domain of ABC7. Login to comment
8 In contrast, the expression of mutated ABC7 (E433K) or Atm1p (D398K) proteins in èc;atm1 cells led to a low efficiency of cytosolic Fe/S protein maturation. Login to comment
160 The mutation resulted in a substitution of lysine for the wild-type glutamate at amino acid 433 (E433K) of the ABC7 protein and abolished a BsmAI restriction site (Figure 1D). Login to comment
165 In addition, we performed similar studies with Atm1p into which the mutation corresponding to the human ABC7 mutant (E433K) was introduced (Atm1p D398K). Login to comment
166 Wild-type Atm1p and, to a slightly lesser extent, ABC7 complemented the growth defect of èc;atm1 cells and the defect leading to mitochondrial iron accumulation.12 Similarly, both the Atm1p D398K and the ABC7 E433K mutant proteins restored growth of èc;atm1 cells to a similar extent as the corresponding wild-type proteins (data not shown). Login to comment
173 Finally, we investigated the consequences of the XLSA/A mutation E433K in ABC7 and the corresponding mutation in Atm1p (D398K) for the function of these proteins in cytosolic Fe/S protein maturation. Login to comment