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Article

Clinical or ATPase domain mutations in ABCD4 disrupt the interaction between the vitamin B12-trafficking proteins ABCD4 and LMBD1.

The Journal of biological chemistry - 14 Jul 2017

Fettelschoss Victoria, Burda Patricie, Sagné Corinne, Coelho David, De Laet Corinne, Lutz Seraina, Suormala Terttu, Fowler Brian, Pietrancosta Nicolas, Gasnier Bruno, Bornhauser Beat, Froese D Sean, Baumgartner Matthias R

Abstract excerpt

Vitamin B12 (cobalamin (Cbl)), in the cofactor forms methyl-Cbl and adenosyl-Cbl, is required for the function of the essential enzymes methionine synthase and methylmalonyl-CoA mutase, respectively. Cbl enters mammalian cells by receptor-mediated endocytosis of protein-bound Cbl followed by lysosomal export of free Cbl to the cytosol and further processing to these cofactor forms. The integral membrane proteins...

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Share to Amino Acid Metabolism, Inborn Errors
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 28572511
DOI: 10.1074/jbc.M117.784819
PMCID: PMC5512089

Genes

ABCD4
LMBRD1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Clinical or ATPase domain mutations in ABCD4 disrupt the interaction between the vitamin B12-trafficking proteins ABCD4 and LMBD1.PMID 28572511Read ↗

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