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- W2789370415 abstract "Magnesium is the most abundant intracellular divalent cation and is involved in over 600 enzymatic reactions including energy metabolism and protein synthesis. Cyclin M (CNNM) has been proposed to function as a Mg transporter. Structurally, CNNM contains an N-terminal extracellular domain, a transmembrane domain, and a large cytosolic region containing a CBS domain and a putative cyclic nucleotide (cNMP)-binding domain. CNNMs interact with oncogenic PRLs (phosphatases of regenerating liver), which are frequently overexpressed in malignant human cancers. When PRL binds CNNM, intracellular Mg level is increased, thereby allowing cancer cells to proliferate. Here, we report the crystal structure of cytosolic domains of CNNM2 and CNNM3. We found that CNNMs dimerize through its C-terminal cNMP-binding domain, and that the CBS domain dimerization is dependent on Mg and ATP binding. Our study provides insights into the mechanism in which CNNM senses intracellular ATP-Mg level and mediate Mg transport." @default.
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- W2789370415 date "2018-02-01" @default.
- W2789370415 modified "2023-09-23" @default.
- W2789370415 title "Structural Studies of Magnesium Transporter CNNM" @default.
- W2789370415 doi "https://doi.org/10.1016/j.bpj.2017.11.3119" @default.
- W2789370415 hasPublicationYear "2018" @default.
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