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- W2600153017 abstract "Abstract Mitochondrial ATP-Mg/Pi carriers import adenine nucleotides into the mitochondrial matrix and export phosphate to the cytosol. They are calcium-regulated to control the size of the matrix adenine nucleotide pool in response to cellular energetic demands. They consist of three domains: an N-terminal regulatory domain containing four calcium-binding EF-hands, a linker loop domain with an amphipathic α-helix and a C-terminal mitochondrial carrier domain for the transport of substrates. Here, we use thermostability assays to demonstrate that the carrier is regulated by calcium via a locking pin mechanism involving the amphipathic α-helix. When calcium levels in the intermembrane space are high, the N-terminus of the amphipathic α-helix is bound to a cleft in the regulatory domain, leading to substrate transport by the carrier domain. When calcium levels drop, the cleft closes, and the amphipathic α-helix is released to bind to the carrier domain via its C-terminus, locking the carrier in an inhibited state." @default.
- W2600153017 created "2017-04-07" @default.
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- W2600153017 date "2017-03-28" @default.
- W2600153017 modified "2023-10-07" @default.
- W2600153017 title "Calcium regulation of the human mitochondrial ATP-Mg/Pi carrier SLC25A24 uses a locking pin mechanism" @default.
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- W2600153017 doi "https://doi.org/10.1038/srep45383" @default.
- W2600153017 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5369052" @default.
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