ArticlePloS one2010
The N-terminal extension domain of the C. elegans half-molecule ABC transporter, HMT-1, is required for protein-protein interactions and function.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 14 citations in OpenAlex.
- CITF1 interacts with FIT and regulates copper-iron crosstalk in Arabidopsis.The Plant cell · 2026Article
- Genome-wide identification of the ABC gene family in sweet potato and its expression profiles in response to iron, aluminum, zinc, and copper stresses.Frontiers in plant science · 2026Article
- Loss of OPT3 function decreases phloem copper levels and impairs crosstalk between copper and iron homeostasis and shoot-to-root signaling in Arabidopsis thaliana.The Plant cell · 2023Article
- Cadmium alters whole animal ionome and promotes the re-distribution of iron in intestinal cells ofFrontiers in physiology · 2023Article
- Cadmium hijacks the high zinc response by binding and activating the HIZR-1 nuclear receptor.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Molecular Responses to Cadmium Exposure in Two Contrasting Durum Wheat Genotypes.International journal of molecular sciences · 2021Article
- Article
- N-Terminal Extension and C-Terminal Domains Are Required for ABCB6/HMT-1 Protein Interactions, Function in Cadmium Detoxification, and Localization to the Endosomal-Recycling System inFrontiers in physiology · 2018Article
- Promotion of bone morphogenetic protein signaling by tetraspanins and glycosphingolipids.PLoS genetics · 2015Article
- Role of the N-terminal transmembrane domain in the endo-lysosomal targeting and function of the human ABCB6 protein.The Biochemical journal · 2015Article
- COPT6 is a plasma membrane transporter that functions in copper homeostasis in Arabidopsis and is a novel target of SQUAMOSA promoter-binding protein-like 7.The Journal of biological chemistry · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMembers of the HMT-1 (heavy metal tolerance factor 1) subfamily of the ATP-binding cassette (ABC) transporter superfamily detoxify heavy metals and have unique topology: they are half-molecule ABC transporters that, in addition to a single transmembrane domain (TMD1) and a single nucleotide-binding domain (NBD1), possess a hydrophobic NH2-terminal extension (NTE). These structural features distinguish HMTs from other ABC transporters in different species including Drosophila and humans. Functional ABC transporters, however, are comprised of at least four-domains (two TMDs and two NDBs) formed from either a single polypeptide or by the association of two or four separate subunits. Whether HMTs act as oligomers and what role the NTE domain plays in their function have not been determined. METHODOLOGY/PRINCIPAL
findingsIn this study, we examined the oligomeric status of Caenorhabditis elegans HMT-1 and the functional significance of its NTE using gel-filtration chromatography in combination with the mating-based split-ubiquitin yeast two-hybrid system (mbSUS) and functional in vivo assays. We found that HMT-1 exists in a protein complex in C. elegans. Studies in S. cerevisiae showed that HMT-1 at a minimum homodimerizes and that oligomerization is essential for HMT-1 to confer cadmium tolerance. We also established that the NTE domain plays an important structural and functional role: it is essential for HMT-1 oligomerization and Cd-detoxification function. However, the NTE itself was not sufficient for oligomerization suggesting that multiple structural features of HMT-1 must associate to form a functional transporter.
conclusionsThe prominence of heavy metals as environmental toxins and the remarkable conservation of HMT-1 structural architecture and function in different species reinforce the value of continued studies of HMT-1 in model systems for identifying functional domains in HMT1 of humans.
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