Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Identification of a novel human subfamily of mitochondrial carriers with calcium-binding domains.
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Characterizes the SCaMC subfamily (including SCaMC-1/SLC25A24); all SCaMC proteins localize exclusively to mitochondria and have an N-terminal EF-hand calcium-binding extension plus a C-terminal mitochondrial carrier domain.
"All SCaMC proteins were found to be located exclusively in mitochondria"
Identification of the mitochondrial ATP-Mg/Pi transporter. Bacterial expression, reconstitution, functional characterization, and tissue distribution.
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Bacterially expressed, reconstituted human ATP-Mg/Pi carrier isoforms transport ATP-Mg in exchange for phosphate and mediate net uptake/efflux of adenine nucleotides, controlling matrix adenine-nucleotide content.
"ATP-Mg is transported in exchange for phosphate"
SCaMC-1 promotes cancer cell survival by desensitizing mitochondrial permeability transition via ATP/ADP-mediated matrix Ca(2+) buffering.
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SCaMC-1/SLC25A24 mediates calcium-triggered ATP-Mg/ADP uptake into mitochondria; the imported ATP/ADP buffer matrix calcium, desensitizing the mitochondrial permeability transition, and knockdown sensitizes cells to oxidative-stress- and calcium-overload-induced necrotic death.
"the mitochondrial carrier SCaMC-1/SLC25A24 mediates ATP-Mg(2-)/Pi(2-) and/or HADP(2-)/Pi(2-) uptake into the mitochondria after an increase in cytosolic"
A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport.
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Crystal structure (PDB 4N5X) plus NMR/SPR show the N-terminal EF-hand domain binds calcium and undergoes a calcium-triggered conformational switch: apo NTD caps and binds the transporter domain (inhibiting transport), while the calcium-bound NTD is self-sequestered and releases it, providing a molecular basis for calcium-dependent ATP-Mg transport.
"Crystal structure of the Ca²⁺-bound NTD reveals a compact architecture in which the functional EF hands are sequestered by an endogenous helical segment"
De Novo Mutations in SLC25A24 Cause a Craniosynostosis Syndrome with Hypertrichosis, Progeroid Appearance, and Mitochondrial Dysfunction.
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Recurrent de novo p.Arg217His/p.Arg217Cys variants in SLC25A24 cause Gorlin- Chaudhry-Moss (Fontaine progeroid) syndrome; patient fibroblasts show mitochondrial swelling exacerbated by H2O2, lower matrix ATP, and increased sensitivity to oxidative stress, indicating a gain of pathological function.
"mitochondrial dysfunction with increased sensitivity to oxidative stress is due to the SLC25A24 mutations"
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.