期刊
SCIENTIFIC REPORTS
卷 7, 期 -, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/srep45383
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资金
- MRC [MC_UU_00015/1, MC_U105663139] Funding Source: UKRI
- Medical Research Council [MC_U105663139, 1095735, MC_UU_00015/1] Funding Source: researchfish
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 alpha-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 alpha-helix. When calcium levels in the intermembrane space are high, the N-terminus of the amphipathic alpha-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 alpha-helix is released to bind to the carrier domain via its C-terminus, locking the carrier in an inhibited state.
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