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Mutations in ABCD4 cause a new inborn error of vitamin B12 metabolism

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Mutations in ABCD4 cause a new inborn error of vitamin B12 metabolism. / Coelho, David; Kim, Jaeseung C; Miousse, Isabelle R; Fung, Stephen; du Moulin, Marcel; Buers, Insa; Suormala, Terttu; Burda, Patricie; Frapolli, Michele; Stucki, Martin; Nürnberg, Peter; Thiele, Holger; Robenek, Horst; Höhne, Wolfgang; Longo, Nicola; Pasquali, Marzia; Mengel, Eugen; Watkins, David; Shoubridge, Eric A; Majewski, Jacek; Rosenblatt, David S; Fowler, Brian; Rutsch, Frank; Baumgartner, Matthias R.

In: NAT GENET, Vol. 44, No. 10, 10.2012, p. 1152-5.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Coelho, D, Kim, JC, Miousse, IR, Fung, S, du Moulin, M, Buers, I, Suormala, T, Burda, P, Frapolli, M, Stucki, M, Nürnberg, P, Thiele, H, Robenek, H, Höhne, W, Longo, N, Pasquali, M, Mengel, E, Watkins, D, Shoubridge, EA, Majewski, J, Rosenblatt, DS, Fowler, B, Rutsch, F & Baumgartner, MR 2012, 'Mutations in ABCD4 cause a new inborn error of vitamin B12 metabolism', NAT GENET, vol. 44, no. 10, pp. 1152-5. https://doi.org/10.1038/ng.2386

APA

Coelho, D., Kim, J. C., Miousse, I. R., Fung, S., du Moulin, M., Buers, I., Suormala, T., Burda, P., Frapolli, M., Stucki, M., Nürnberg, P., Thiele, H., Robenek, H., Höhne, W., Longo, N., Pasquali, M., Mengel, E., Watkins, D., Shoubridge, E. A., ... Baumgartner, M. R. (2012). Mutations in ABCD4 cause a new inborn error of vitamin B12 metabolism. NAT GENET, 44(10), 1152-5. https://doi.org/10.1038/ng.2386

Vancouver

Coelho D, Kim JC, Miousse IR, Fung S, du Moulin M, Buers I et al. Mutations in ABCD4 cause a new inborn error of vitamin B12 metabolism. NAT GENET. 2012 Oct;44(10):1152-5. https://doi.org/10.1038/ng.2386

Bibtex

@article{84552f7f7b0945ae9f3fb58f699f4d93,
title = "Mutations in ABCD4 cause a new inborn error of vitamin B12 metabolism",
abstract = "Inherited disorders of vitamin B12 (cobalamin) have provided important clues to how this vitamin, which is essential for hematological and neurological function, is transported and metabolized. We describe a new disease that results in failure to release vitamin B12 from lysosomes, which mimics the cblF defect caused by LMBRD1 mutations. Using microcell-mediated chromosome transfer and exome sequencing, we identified causal mutations in ABCD4, a gene that codes for an ABC transporter, which was previously thought to have peroxisomal localization and function. Our results show that ABCD4 colocalizes with the lysosomal proteins LAMP1 and LMBD1, the latter of which is deficient in the cblF defect. Furthermore, we show that mutations altering the putative ATPase domain of ABCD4 affect its function, suggesting that the ATPase activity of ABCD4 may be involved in intracellular processing of vitamin B12.",
keywords = "ATP-Binding Cassette Transporters, Abnormalities, Multiple, Case-Control Studies, Cells, Cultured, DNA Mutational Analysis, Fibroblasts, Gene Expression, Genes, Recessive, Genetic Association Studies, Humans, Infant, Newborn, Lysosome-Associated Membrane Glycoproteins, Metabolism, Inborn Errors, Mutation, Nucleocytoplasmic Transport Proteins, Protein Structure, Tertiary, Protein Transport, Vitamin B 12, Journal Article, Research Support, Non-U.S. Gov't",
author = "David Coelho and Kim, {Jaeseung C} and Miousse, {Isabelle R} and Stephen Fung and {du Moulin}, Marcel and Insa Buers and Terttu Suormala and Patricie Burda and Michele Frapolli and Martin Stucki and Peter N{\"u}rnberg and Holger Thiele and Horst Robenek and Wolfgang H{\"o}hne and Nicola Longo and Marzia Pasquali and Eugen Mengel and David Watkins and Shoubridge, {Eric A} and Jacek Majewski and Rosenblatt, {David S} and Brian Fowler and Frank Rutsch and Baumgartner, {Matthias R}",
year = "2012",
month = oct,
doi = "10.1038/ng.2386",
language = "English",
volume = "44",
pages = "1152--5",
journal = "NAT GENET",
issn = "1061-4036",
publisher = "NATURE PUBLISHING GROUP",
number = "10",

}

RIS

TY - JOUR

T1 - Mutations in ABCD4 cause a new inborn error of vitamin B12 metabolism

AU - Coelho, David

AU - Kim, Jaeseung C

AU - Miousse, Isabelle R

AU - Fung, Stephen

AU - du Moulin, Marcel

AU - Buers, Insa

AU - Suormala, Terttu

AU - Burda, Patricie

AU - Frapolli, Michele

AU - Stucki, Martin

AU - Nürnberg, Peter

AU - Thiele, Holger

AU - Robenek, Horst

AU - Höhne, Wolfgang

AU - Longo, Nicola

AU - Pasquali, Marzia

AU - Mengel, Eugen

AU - Watkins, David

AU - Shoubridge, Eric A

AU - Majewski, Jacek

AU - Rosenblatt, David S

AU - Fowler, Brian

AU - Rutsch, Frank

AU - Baumgartner, Matthias R

PY - 2012/10

Y1 - 2012/10

N2 - Inherited disorders of vitamin B12 (cobalamin) have provided important clues to how this vitamin, which is essential for hematological and neurological function, is transported and metabolized. We describe a new disease that results in failure to release vitamin B12 from lysosomes, which mimics the cblF defect caused by LMBRD1 mutations. Using microcell-mediated chromosome transfer and exome sequencing, we identified causal mutations in ABCD4, a gene that codes for an ABC transporter, which was previously thought to have peroxisomal localization and function. Our results show that ABCD4 colocalizes with the lysosomal proteins LAMP1 and LMBD1, the latter of which is deficient in the cblF defect. Furthermore, we show that mutations altering the putative ATPase domain of ABCD4 affect its function, suggesting that the ATPase activity of ABCD4 may be involved in intracellular processing of vitamin B12.

AB - Inherited disorders of vitamin B12 (cobalamin) have provided important clues to how this vitamin, which is essential for hematological and neurological function, is transported and metabolized. We describe a new disease that results in failure to release vitamin B12 from lysosomes, which mimics the cblF defect caused by LMBRD1 mutations. Using microcell-mediated chromosome transfer and exome sequencing, we identified causal mutations in ABCD4, a gene that codes for an ABC transporter, which was previously thought to have peroxisomal localization and function. Our results show that ABCD4 colocalizes with the lysosomal proteins LAMP1 and LMBD1, the latter of which is deficient in the cblF defect. Furthermore, we show that mutations altering the putative ATPase domain of ABCD4 affect its function, suggesting that the ATPase activity of ABCD4 may be involved in intracellular processing of vitamin B12.

KW - ATP-Binding Cassette Transporters

KW - Abnormalities, Multiple

KW - Case-Control Studies

KW - Cells, Cultured

KW - DNA Mutational Analysis

KW - Fibroblasts

KW - Gene Expression

KW - Genes, Recessive

KW - Genetic Association Studies

KW - Humans

KW - Infant, Newborn

KW - Lysosome-Associated Membrane Glycoproteins

KW - Metabolism, Inborn Errors

KW - Mutation

KW - Nucleocytoplasmic Transport Proteins

KW - Protein Structure, Tertiary

KW - Protein Transport

KW - Vitamin B 12

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1038/ng.2386

DO - 10.1038/ng.2386

M3 - SCORING: Journal article

C2 - 22922874

VL - 44

SP - 1152

EP - 1155

JO - NAT GENET

JF - NAT GENET

SN - 1061-4036

IS - 10

ER -